Journal of structural biology最新文献_第3页

High-Resolution single particle analysis using a scintillator camera XF416 on CRYOARM300II at 300 kV 在300 kV的CRYOARM300II上使用闪烁体相机XF416进行高分辨率单粒子分析。

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2026-03-01 Epub Date: 2026-01-03 DOI: 10.1016/j.jsb.2026.108286

Shinji Aramaki , Tomohito Tanihara , Yuya Yoshida , Naoya Matsunaga , Shigehiro Ohdo , Kouta Mayanagi

{"title":"High-Resolution single particle analysis using a scintillator camera XF416 on CRYOARM300II at 300 kV","authors":"Shinji Aramaki , Tomohito Tanihara , Yuya Yoshida , Naoya Matsunaga , Shigehiro Ohdo , Kouta Mayanagi","doi":"10.1016/j.jsb.2026.108286","DOIUrl":"10.1016/j.jsb.2026.108286","url":null,"abstract":"<div><div>The advent of direct electron detectors (DEDs) has driven a major breakthrough in cryo-electron microscopy (cryo-EM), particularly in single-particle analysis (SPA), establishing DEDs as essential tools for achieving near-atomic resolution. In this study, we re-evaluated the performance of the TVIPS TemCam-XF416, an indirect scintillator-coupled CMOS camera (scintillator camera). Using a JEOL CRYOARM 300II, we performed SPA on two well-established benchmark specimens, β-galactosidase and apoferritin, at a 300 kV acceleration voltage. The resulting reconstructions reached resolutions of 2.6 Å and 2.1 Å, respectively. Notably, the apoferritin map clearly resolves the central holes of aromatic side chains—a level of detail previously considered exclusive to DEDs. These results were achieved by implementing the latest standard reconstruction workflows, including motion correction and contrast transfer function refinement, underscoring the critical role of computational methods in attaining high-resolution structures. While scintillator cameras inherently exhibit a lower signal-to-noise ratio than DEDs, our findings with XF416 demonstrate that, with appropriate data collection and processing, such cameras can deliver near-atomic resolution structures. This work establishes a crucial technical benchmark for the scintillator camera evaluated in this study on a high-end 300 kV cryo-EM platform, demonstrating its capability to achieve resolutions suitable for many structural biology applications and providing an updated perspective on its performance capabilities.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"218 1","pages":"Article 108286"},"PeriodicalIF":2.7,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145906274","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Robust mitochondria segmentation and morphological profiling using soft X-ray tomography 稳健的线粒体分割和形态分析使用软x射线断层扫描。

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2026-03-01 Epub Date: 2026-01-08 DOI: 10.1016/j.jsb.2026.108291

Arun Yadav , Anshu Singh , Aneesh Deshmukh , Pushkar Bharadwaj , Anuj Baliyan , Kate White , Jitin Singla

{"title":"Robust mitochondria segmentation and morphological profiling using soft X-ray tomography","authors":"Arun Yadav , Anshu Singh , Aneesh Deshmukh , Pushkar Bharadwaj , Anuj Baliyan , Kate White , Jitin Singla","doi":"10.1016/j.jsb.2026.108291","DOIUrl":"10.1016/j.jsb.2026.108291","url":null,"abstract":"<div><div>Mitochondrial morphology is central to cellular function, yet large-scale quantification is limited by the lack of high-resolution whole-cell imaging and efficient segmentation tools. Soft X-ray tomography (SXT) provides native-state 3D whole-cells images, but organelle segmentation remains a bottleneck. We present MitoXRNet, a data- and parameter-efficient 3D deep learning model for mitochondria and nucleus segmentation in SXT tomograms. Using multi-axis 3D slicing, Sobel filter-based boundary enhancement, and a combined Binary-Cross-Entropy and Robust-Dice loss, MitoXRNet achieves a 73.8% Dice score on INS-1E cells with only 1.4 M parameters, outperforming existing methods. A larger 22.6 M variant generalized well to unseen data. Automated segmentation enabled quantitative analysis of mitochondrial remodeling under metabolic stimuli: glucose increased mitochondrial volume and matrix density, while GIP and GKA increased mitochondria number, reduced volume, and elevated density, indicating smaller, denser, more dynamic populations. MitoXRNet provides a scalable framework for high-throughput morphological and biophysical profiling of organelles in native-state SXT data.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"218 1","pages":"Article 108291"},"PeriodicalIF":2.7,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145949009","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

GNN2Pfam: Integrating protein sequence and structure with graph neural networks for Pfam domain annotation GNN2Pfam：将蛋白质序列和结构与图神经网络相结合，用于Pfam结构域标注。

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2026-03-01 Epub Date: 2026-02-02 DOI: 10.1016/j.jsb.2026.108294

Emilio Fenoy, Leandro A. Bugnon, Rosario Vitale, Sofia A. Duarte, Diego H. Milone, Georgina Stegmayer

{"title":"GNN2Pfam: Integrating protein sequence and structure with graph neural networks for Pfam domain annotation","authors":"Emilio Fenoy, Leandro A. Bugnon, Rosario Vitale, Sofia A. Duarte, Diego H. Milone, Georgina Stegmayer","doi":"10.1016/j.jsb.2026.108294","DOIUrl":"10.1016/j.jsb.2026.108294","url":null,"abstract":"<div><div>The challenge of establishing the relationship between protein sequences and their function cannot yet be considered completely solved. State-of-the-art annotation of Pfam domains is based on hidden Markov models (HMMs) built from hand-crafted sequence alignments. However, while this approach has been highly successful during the last decades since its proposal, there is yet a very large number of proteins that remain unannotated because there is no possible alignment to already known and functionally characterized sequences, or HMM fails to discriminate between similar domains. Adding structural information using deep and graph neural networks (GNNs) presents an opportunity to build upon existing models in those more challenging cases. GNNs excel at capturing complex relationships in data and can learn a model that shares information across all existing families, thus being able to generalize Pfam domain predictions to novel sequences. In this protocol we propose GNN2Pfam, an end-to-end GNN-based method for Pfam family domain annotation. Our strategy allows one single model to be trained for all species and families. This novel proposal uses the protein 3D structure together with a sequence representation obtained from a large pre-trained model. The GNN2Pfam method is based on a graph derived from amino acid interactions in the 3D structure, learning both sequential and structural features from this representation. Experiments show that the proposed GNN-based model can clearly outperform the HMM state-of-the-art predictive performance in Pfam domains annotations. These results suggest that GNN models can be the key component of future protein annotation tools. Data and source code are available at <span><span>https://github.com/efenoy/GNN2Pfam</span><svg><path></path></svg></span>.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"218 1","pages":"Article 108294"},"PeriodicalIF":2.7,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146113417","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural features of collagens of warm-blooded and cold-blooded animals that determine differences in their thermal stability 温血动物和冷血动物胶原蛋白的结构特征决定了它们热稳定性的差异

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2026-03-01 Epub Date: 2026-01-26 DOI: 10.1016/j.jsb.2026.108295

Olga V. Meshcheryakova , Maxim A. Bogdanov , Alexander V. Efimov

{"title":"Structural features of collagens of warm-blooded and cold-blooded animals that determine differences in their thermal stability","authors":"Olga V. Meshcheryakova , Maxim A. Bogdanov , Alexander V. Efimov","doi":"10.1016/j.jsb.2026.108295","DOIUrl":"10.1016/j.jsb.2026.108295","url":null,"abstract":"<div><div>We have previously shown that the thermal stability of animal collagens correlates with the number of hydrophobic amino acid residues in their composition: the more hydrophobic residues in a molecule, the higher the denaturation temperature of collagen. In addition, it was found that with the same hydrophobicity, the thermal stability of collagens of cold-blooded animals can be several degrees lower than that of warm-blooded animals. To understand the reasons for this, we studied the amino acid composition and sequences of α1, α2, and α3 chains of type I collagen in warm-blooded and cold-blooded animals. The α3 chain is found only in cold-blooded animals and is represented by sequences for only 6 fish species. The results of the study show that differences in the thermal stability of collagens of warm-blooded and cold-blooded animals may be due to differences in the number of Gly-Gly pairs, Pro, Ala, Met, Ser in collagen subunits. A negative correlation was observed between the number of GGY (Gly-Gly-Yaa, pair Gly-Gly is before Yaa in the sequence) and GGX (pair Gly-Gly is before Xaa in the sequence) and collagen thermal stability. Differences in the amounts of GGY and GGX were also observed between the different types of α1, α2, and α 3 chains. A negative correlation with thermal stability was also observed for Ser. For all chain types, the amount of Pro at position Xaa and Pro at position Yaa was shown to correlate with collagen denaturation temperatures. Moreover, in the α1 and α2 chains of warm-blooded and cold-blooded animals, the positive correlation with Pro(Yaa) was higher than with Pro (Xaa). Similarities were found between the α1 and α3 chains and their differences from the α2 chain in the amount and ratio of Pro (Xaa) and Pro (Yaa).</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"218 1","pages":"Article 108295"},"PeriodicalIF":2.7,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146090154","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A Multi-Technique Investigation to Explore the Structural Integrity and Chemical Complexity of the Brachiopod Lingula anatina (Lamarck, 1801) Shells 利用多种技术研究腕足动物Lingula anatina （Lamarck, 1801）壳的结构完整性和化学复杂性。

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2025-12-01 Epub Date: 2025-09-13 DOI: 10.1016/j.jsb.2025.108248

Prabad Pratim Pal, Sourav Bar, Santosh Kumar Bera, Debkumar Sahoo, Sudipta Kumar Ghorai

{"title":"A Multi-Technique Investigation to Explore the Structural Integrity and Chemical Complexity of the Brachiopod Lingula anatina (Lamarck, 1801) Shells","authors":"Prabad Pratim Pal, Sourav Bar, Santosh Kumar Bera, Debkumar Sahoo, Sudipta Kumar Ghorai","doi":"10.1016/j.jsb.2025.108248","DOIUrl":"10.1016/j.jsb.2025.108248","url":null,"abstract":"<div><div>The shell of <em>Lingula anatina</em>, a living representative of early brachiopods, exemplifies a unique organophosphatic biomineralization strategy that integrates mineral phases with organic components for structural enhancement. This study employs scanning electron microscopy (SEM), energy-dispersive X-ray spectroscopy (EDS), inductively coupled plasma optical emission spectrometry (ICP-OES), X-ray diffraction (XRD), and Raman spectroscopy to comprehensively analyse the microstructure, composition, and mineralogy of the shell. SEM imaging reveals distinct regional microarchitectures, from compact fibrous laminae to porous, reticulate layers, indicating functional specialization in structural reinforcement and flexibility. Elemental analyses confirm a calcium-phosphate matrix dominated by fluorapatite and enriched with trace elements like Mg, Mn, and Fe. XRD and Raman data validate the coexistence of crystalline fluorapatite and calcite with significant amorphous phases. These findings highlight <em>Lingula’s</em> evolutionary retention of a hierarchical, organic–inorganic composite shell adapted for environmental interaction, structural resilience, and biomineral control.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"217 4","pages":"Article 108248"},"PeriodicalIF":2.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145069874","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Announcement: Journal of Structural Biology: Paper of the year 公告：结构生物学杂志：年度论文。

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2025-12-01 Epub Date: 2025-11-24 DOI: 10.1016/j.jsb.2025.108263

Moon Ki Kim

引用次数: 0

Hurdles and advancements in experimental membrane protein structural biology 实验膜蛋白结构生物学的障碍与进展。

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2025-12-01 Epub Date: 2025-09-28 DOI: 10.1016/j.jsb.2025.108251

Ruchika Bajaj

{"title":"Hurdles and advancements in experimental membrane protein structural biology","authors":"Ruchika Bajaj","doi":"10.1016/j.jsb.2025.108251","DOIUrl":"10.1016/j.jsb.2025.108251","url":null,"abstract":"<div><div>This short review article traces the evolution of membrane protein structural biology over time and describes various challenges faced and overcome by researchers in the field, highlighting some of the major breakthroughs and advancements in the field. It presents a thematic exploration of membrane protein structural biology emphasizing on persistent technical and conceptual challenges from protein expression to structural techniques shaping the field with landmark innovations advancing our ability to determine membrane protein structures. The review specifically focus on a few key areas: sourcing and expressing membrane proteins, developing purification strategies and membrane mimetics, and the emergence of powerful structural tools such as X-ray crystallography, cryo-electron microscopy (cryo-EM) and micro-electron diffraction (MicroED). Each section discusses major advancements addressing long standing bottlenecks and opening avenues to understand structure–function relationships in membrane proteins. Furthermore, it also briefly discusses the impact of important discoveries and future perspectives for the field. The review concludes by discussing current emerging frontiers in the field including <em>in-situ</em> structural methods, AI driven structure prediction and future directions for integrative and dynamic membrane protein research.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"217 4","pages":"Article 108251"},"PeriodicalIF":2.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145199956","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cholesterol crystals in reservosomes of Trypanosoma cruzi 克氏锥虫水库中的胆固醇结晶。

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2025-12-01 Epub Date: 2025-10-30 DOI: 10.1016/j.jsb.2025.108259

Heloá Estevam , Rodrigo T. Carvalho , Leonardo T. Salgado , Carolina L. Alcantara , Jessica Aguiar-Seabra , Wanderley de Souza , Narcisa L. Cunha-e-Silva , Miria G. Pereira

{"title":"Cholesterol crystals in reservosomes of Trypanosoma cruzi","authors":"Heloá Estevam , Rodrigo T. Carvalho , Leonardo T. Salgado , Carolina L. Alcantara , Jessica Aguiar-Seabra , Wanderley de Souza , Narcisa L. Cunha-e-Silva , Miria G. Pereira","doi":"10.1016/j.jsb.2025.108259","DOIUrl":"10.1016/j.jsb.2025.108259","url":null,"abstract":"<div><div>The LDL endocytosis provides cholesterol supply to <em>Trypanosoma cruzi</em> epimastigotes. Cholesterol reaches reservosomes (lysosome like organelles) being used according to cell demand or is storage in lipid droplets. But a remnant fraction remains in reservosome lumen where solidifies. In this work we investigated the crystalline properties of these cholesterol solids. First, ultrathin sections, freeze fracture and deep etching replicas suggested collectively different spatial configurations such as needles, plaques or rounded structures. Cryo-EM images showed hemi- and membrane profiles in close association with sterol solids, possibly flanking the growth of these structures. Second, the analysis <em>in situ</em> of parasites by polarized light microscopy pointed to the birefringence of cholesterol. In this way, we used fractions of reservosome lipid inclusions to determine the spectral signature by FTIR, and X-ray diffraction defined the crystallinity of the lipid inclusions. Additionally, our analyses showed that cholesterol was arranged in two polymorphs of anhydrous crystal. Cholesterol crystals had triclinic configuration. Polymorph 1 presented the following unit cell parameters: <em>a</em> = 14.21Å, <em>b</em> = 33.86Å, <em>c</em> = 10.56Å, <em>V</em> = 5028.8Å while the polymorph 2: <em>a</em> = 27.32 Å, <em>b</em> = 38.24 Å, <em>c</em> = 10.66 Å, <em>V</em> = 9776.98 Å. Differences in crystalline densities were also found by our group. The polymorph 1 was more packed and denser than the second crystal analyzed. The densities were estimated in 5.11 g/cm<sup>3</sup> and 2.63 g/cm<sup>3</sup>, respectively. Third, cholesterol crystals did not impair metacyclogenesis being rapidly dismantled if parasites were kept under nutritional starvation.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"217 4","pages":"Article 108259"},"PeriodicalIF":2.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145426923","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural insights into IMP2 dimerization and RNA binding IMP2二聚化和RNA结合的结构见解

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2025-12-01 Epub Date: 2025-09-12 DOI: 10.1016/j.jsb.2025.108247

Stephen A. Zorc , Paola Munoz-Tello , Timothy O’Leary , Xiaoyu Yu , Mithun Nag Karadi Giridhar , Alexander D. Hondros , Althea Hansel-Harris , Stefano Forli , Patrick R. Griffin , Douglas J. Kojetin , Raktim N. Roy , Michalina Janiszewska

{"title":"Structural insights into IMP2 dimerization and RNA binding","authors":"Stephen A. Zorc , Paola Munoz-Tello , Timothy O’Leary , Xiaoyu Yu , Mithun Nag Karadi Giridhar , Alexander D. Hondros , Althea Hansel-Harris , Stefano Forli , Patrick R. Griffin , Douglas J. Kojetin , Raktim N. Roy , Michalina Janiszewska","doi":"10.1016/j.jsb.2025.108247","DOIUrl":"10.1016/j.jsb.2025.108247","url":null,"abstract":"<div><div>IGF2BP2 (IMP2) is an RNA-binding protein that contributes to tumorigenesis and metabolic disorders. Structural studies focused on individual IMP2 domains have provided important mechanistic insights into IMP2 function; however, structural information on full-length IMP2 is lacking but necessary to understand how to target IMP2 activity in drug discovery. In this study, we investigated the behavior of full-length IMP2 and the influence of RNA binding using biophysical and structural methods including mass photometry, hydrogen–deuterium exchange coupled to mass spectrometry (HDX-MS), and small angle x-ray scattering (SAXS). We found that full-length IMP2 forms multiple oligomeric states but predominantly adopts a dimeric conformation. Molecular models derived from SAXS data suggest the dimer is formed in a head-to-tail orientation by the KH34 and RRM1 domains. Upon RNA binding, IMP2 forms a pseudo-symmetric dimer different from its apo/RNA-free state. We also found that the formation of IMP2 oligomeric species, which includes dimers and higher-order oligomers, is sensitive to ionic strength and RNA binding. Our findings provide the first insight into the structural properties of full-length IMP2, which may lead to novel opportunities for disrupting its function.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"217 4","pages":"Article 108247"},"PeriodicalIF":2.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145047686","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

CDP-alcohol phosphotransferases: Structures and function of highly diverse sub-classes within a protein family cdp -醇磷酸转移酶：蛋白质家族中高度不同亚类的结构和功能

IF 2.7 3区生物学

Journal of structural biology Pub Date : 2025-12-01 Epub Date: 2025-11-25 DOI: 10.1016/j.jsb.2025.108266

Alexia Gobet, Rasmus Kock Flygaard

{"title":"CDP-alcohol phosphotransferases: Structures and function of highly diverse sub-classes within a protein family","authors":"Alexia Gobet, Rasmus Kock Flygaard","doi":"10.1016/j.jsb.2025.108266","DOIUrl":"10.1016/j.jsb.2025.108266","url":null,"abstract":"<div><div>Membranes are essential components of cells and their compartments. They are composed of asymmetric phospholipid bilayers that separate different environments ensuring the physiological functioning of cells. Most phospholipids are synthesized in the endoplasmic reticulum and transported to the target membrane via various routes. Phosphatidic acid is the starting point for all lipid synthesis pathways, following either the Kennedy pathway for phosphatidylserine, phosphatidylethanolamine and phosphatidylcholine or the CDP-DAG pathway for cardiolipin, phosphatidylglycerol and phosphatidylinositol. Many of the enzymes responsible for these synthesis pathways belong to the cytidine diphosphate alcohol phosphotransferase (CDP-AP) family for which a detailed structural and functional understanding is missing. In this review, we focus on the CDP-AP protein family which is divided in two classes, defined by different structures and mechanisms. The CDP-AP members are membrane proteins, and their mode of catalysis follows a bi-bi or ping-pong mechanism. Recent studies on different CDP-AP family members are bringing new molecular insights on these essential proteins.</div></div><div><h3>Teaser</h3><div>CDP-alcohol phosphotransferase proteins are highly diverged in structure while their overall function in phospholipid synthesis is conserved.</div></div>","PeriodicalId":17074,"journal":{"name":"Journal of structural biology","volume":"217 4","pages":"Article 108266"},"PeriodicalIF":2.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145619936","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0