Acta crystallographica. Section F, Structural biology communications最新文献

Recombinant versus native botulinum neurotoxin type A: structural and pharmacodynamic comparison. 重组与天然A型肉毒杆菌神经毒素：结构和药效学比较。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-11-01 Epub Date: 2026-10-22 DOI: 10.1107/S2053230X26009830

Zongren Yao, Lingyi Xu, Yu Lu, Hui Gong, Xiaoyun Sun, Yaokun Zhao, Jinhuan Chen, Liming Yang, Qingqing Chen, Wu Yang

{"title":"Recombinant versus native botulinum neurotoxin type A: structural and pharmacodynamic comparison.","authors":"Zongren Yao, Lingyi Xu, Yu Lu, Hui Gong, Xiaoyun Sun, Yaokun Zhao, Jinhuan Chen, Liming Yang, Qingqing Chen, Wu Yang","doi":"10.1107/S2053230X26009830","DOIUrl":"10.1107/S2053230X26009830","url":null,"abstract":"Botulinum neurotoxins (BoNTs) are highly potent exotoxins utilized for esthetic and therapeutic indications. Unlike traditional products derived from Clostridium botulinum, this study presents the design, production, structural characterization and preclinical pharmacodynamics of recombinant BoNT type A1 (rBoNT/A, YY001), newly approved by the National Medical Products Administration and the first rBoNT/A product to be licensed for commercialization in the world. Expressed in Escherichia coli and purified to greater than 99% homogeneity, YY001 shares a core amino-acid sequence with BoNT/A1 in Botox. The additional five residues at the N-terminus and six residues at the C-terminus of the light chain (LC), as well as two residues at the N-terminus of the heavy chain (HC), originate from residual amino acids after protease cleavage; mass-spectrometric peptide mapping confirmed this sequence fidelity. Cryo-electron microscopy yields a 3.2 Å resolution map of the full-length active rBoNT/A, revealing a canonical LC-HN-HC three-domain architecture that predominantly adopts an open conformation, with a root-mean-square deviation of 1.3-1.5 Å relative to native BoNT/A. In vivo head-to-head pharmacodynamic studies showed comparable potency between YY001 and Botox in both mouse digit abduction score assay and rat compound muscle action potential assays. Altogether, the structural, biochemical and pharmacological data indicate that YY001 possesses molecular and functional attributes that are highly comparable to those of native BoNT/A, while providing improved manufacturing consistency and reduced biosafety risks.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"391-401"},"PeriodicalIF":1.1,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13717837/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149242481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

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Crystal structure of the bifunctional enzyme phosphoribosyl isomerase A from Mycobacterium tuberculosis with bound light-controllable inhibitor. 结合光可控抑制剂的结核分枝杆菌双功能酶磷酸核糖基异构酶A的晶体结构。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-11-01 Epub Date: 2026-10-12 DOI: 10.1107/S2053230X26009684

Chitra Rajendran, Reinhard Sterner

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Structural analysis of Helicobacter pylori glutamate racemase in a monoclinic crystal form. 单斜晶型幽门螺杆菌谷氨酸消旋酶的结构分析。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-11-01 Epub Date: 2026-10-09 DOI: 10.1107/S2053230X26008782

Maria Spiliopoulou, Eike C Schulz

{"title":"Structural analysis of Helicobacter pylori glutamate racemase in a monoclinic crystal form.","authors":"Maria Spiliopoulou, Eike C Schulz","doi":"10.1107/S2053230X26008782","DOIUrl":"10.1107/S2053230X26008782","url":null,"abstract":"Glutamate racemase (MurI) catalyzes the stereochemical interconversion of L-glutamate and D-glutamate, a key element of bacterial peptidoglycan biosynthesis. In this study, we present the crystal structure of Helicobacter pylori glutamate racemase at 1.43 Å resolution and with monoclinic symmetry, as in previously reported models, but with different unit-cell parameters. The present model contains a single dimer in the asymmetric unit and retains the previously described head-to-head dimer arrangement. Comparative analysis of crystal packing reveals that the conserved dimeric assembly frequently adopts similar packing motifs, while differences in the relative arrangement of these dimeric arrays result in altered crystal packing and variations in unit-cell parameters. The monomeric fold and active-site architecture remain conserved and are consistent with the catalytic features described for bacterial glutamate racemases. This structure provides an updated, high-resolution structural model for H. pylori glutamate racemase and highlights the variability of crystal-packing arrangements within related monoclinic crystal forms.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"376-384"},"PeriodicalIF":1.1,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13717826/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149134693","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Crystal structure of tyrosine-tRNA synthetase from Helicobacter pylori G27. 幽门螺杆菌G27酪氨酸- trna合成酶的晶体结构。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-11-01 Epub Date: 2026-10-23 DOI: 10.1107/S2053230X26010253

David Igbalajobi, Jason E Taylor, Raymond Gao, Jesuferanmi Ayanlade, Rachael Zigweid, Sandhya Subramanian, Hannah Udell, Thomas E Edwards, Jan Abendroth, Donald Lorimer, Peter J Myler, Bart Staker, Edmund Moses Ndip, Oluwatoyin A Asojo

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Crystal structures of the N-terminal and C-terminal domains of the SARS-CoV-2 nucleocapsid protein SARS-CoV-2核衣壳蛋白n端和c端结构域的晶体结构。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-10-29 Epub Date: 2026-10-09 DOI: 10.1107/S2053230X26010058

Xiaojing Song, Georges Chalhoub, Peter J. McCormick, Tingting Hu, Jian Li

{"title":"Crystal structures of the N-terminal and C-terminal domains of the SARS-CoV-2 nucleocapsid protein","authors":"Xiaojing Song, Georges Chalhoub, Peter J. McCormick, Tingting Hu, Jian Li","doi":"10.1107/S2053230X26010058","DOIUrl":"10.1107/S2053230X26010058","url":null,"abstract":"The nucleocapsid (N) protein of Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) functions in viral RNA binding, genome packaging and ribonucleoprotein (RNP) assembly. Crystal structures were determined of the N-terminal domain (NTD) from crystals grown at pH 8.0 to a resolution of 1.94 Å and of the C-terminal domain (CTD) from crystals grown at pH 5.0 and 8.5 to resolutions of 1.59 and 1.30 Å, respectively. The NTD adopts the canonical coronavirus NTD fold and contains a positively charged cleft corresponding to a previously proposed RNA-binding region. Comparison of the apo NTD structure determined in this study with a previously reported RNA-bound NTD structure revealed local differences in the side-chain conformations of RNA-contacting residues, including Thr49, Arg88, Arg92, Arg107, Tyr109 and Tyr111, whereas the overall domain fold remained essentially unchanged. These observations suggest that RNA binding may be accommodated by local side-chain rearrangements within a pre-existing positively charged cleft rather than by a large-scale conformational change. The CTD forms a domain-swapped dimer mediated by β-hairpins, with a positively charged groove extending across the dimer interface. Superposition of the two CTD structures yielded a root-mean-square deviation (r.m.s.d.) of 0.129 Å, and 11 intersubunit hydrogen bonds were observed at the dimer interface in each structure, indicating that the dimer architecture is conserved under the crystallization conditions examined. Together, these structures provide a framework for further investigation of NTD–RNA recognition, the possible role of the CTD positively charged groove in nucleic acid interactions and N-protein assembly.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 11","pages":"402-409"},"PeriodicalIF":1.1,"publicationDate":"2026-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149134736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

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X-ray structure of the human Nijmegen breakage syndrome forkhead-associated/BRCA1 C-terminal domain and computational docking of candidate radiosensitizers 人类奈梅亨断裂综合征叉头相关/BRCA1 c端结构域的x射线结构及候选放射致敏物的计算对接

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-10-29 DOI: 10.1107/S2053230X26010204

Masaki Unno, Kenichi Kitanishi, Kenji Ite, Makiko Ishihara, Rina Sugiyama, Saki Komuro, Keiji Suzuki, Hiroshi Tauchi

{"title":"X-ray structure of the human Nijmegen breakage syndrome forkhead-associated/BRCA1 C-terminal domain and computational docking of candidate radiosensitizers","authors":"Masaki Unno, Kenichi Kitanishi, Kenji Ite, Makiko Ishihara, Rina Sugiyama, Saki Komuro, Keiji Suzuki, Hiroshi Tauchi","doi":"10.1107/S2053230X26010204","DOIUrl":"10.1107/S2053230X26010204","url":null,"abstract":"Nijmegen breakage syndrome 1 (NBS1) forms the MRE11–RAD50–NBS1 complex and is essential for homologous recombination repair of DNA double-strand breaks. NBS1 regulates the localization and activity of the MRN complex. The NBS1 forkhead-associated (FHA) domain represents a potential target for the development of radiosensitizers. However, detailed structural information on the N-terminal region of human NBS1 (hNBS1) is still lacking. Here, the X-ray structure of the hNBS1 FHA–BRCA1 C-terminal (BRCT1)–BRCT2 domains is reported and ligand binding is evaluated using computational docking. A candidate radiosensitizer was predicted to bind at the tip of the FHA domain, indicating a potential interaction site. Substitution of Arg28 with aspartic acid within the FHA domain altered the orientation of neighboring side chains and modified the surface electrostatic properties, supporting its structural and functional importance. These findings provide a structural basis for targeting NBS1 and may facilitate the development of radiosensitizers.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 11","pages":"410-424"},"PeriodicalIF":1.1,"publicationDate":"2026-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149190488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

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IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-10-29

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IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-10-29

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Structure of the cupin protein GloB from Pseudomonas aeruginosa at 1.48 Å resolution 1.48 Å分辨率下铜绿假单胞菌cupin蛋白GloB的结构。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-10-29 DOI: 10.1107/S2053230X26010514

Carlos Contreras-Martel, Kevin Duarte, Pauline Macheboeuf

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IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-10-12

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