Acta crystallographica. Section F, Structural biology communications最新文献_第5页

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-07

引用次数: 0

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-07

引用次数: 0

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-01

引用次数: 0

Optimized bacterial expression of a synthetic BRIL antibody. 优化合成BRIL抗体的细菌表达。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-01 Epub Date: 2026-03-17 DOI: 10.1107/S2053230X26001548

Benjamin F Cooper, Georgia L Isom

引用次数: 0

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-01

引用次数: 0

Structures of pentatricopeptide repeat proteins. 五肽重复蛋白的结构。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-01 Epub Date: 2026-03-30 DOI: 10.1107/S2053230X26002311

Anuradha Pullakhandam, Crystal Cooper, Ian D Small, Charles S Bond

{"title":"Structures of pentatricopeptide repeat proteins.","authors":"Anuradha Pullakhandam, Crystal Cooper, Ian D Small, Charles S Bond","doi":"10.1107/S2053230X26002311","DOIUrl":"10.1107/S2053230X26002311","url":null,"abstract":"Pentatricopeptide repeat (PPR) proteins constitute the largest family of RNA-binding proteins in land plants, playing crucial roles in organellar gene expression through sequence-specific RNA recognition. Including the first PPR crystal structure in 2013, 30 PPR and 83 ribosomal PPR crystal or cryo-EM structures have been deposited in the Protein Data Bank, encompassing both native and designer proteins in apo and RNA-bound states. This comprehensive survey catalogues all PPR crystal structures, analysing their crystallographic properties, structural features and contributions to understanding PPR function. Key insights include the elucidation of the PPR recognition code, the characterization of dramatic conformational changes upon RNA binding and the structural basis for the modular architecture that enables programmable RNA targeting. Designer PPR structures have validated and extended principles derived from native proteins, demonstrating their utility as synthetic biology tools. This structural catalogue provides crystallographers and plant biologists with a comprehensive resource for understanding PPR protein architecture and function.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 Pt 4","pages":"101-113"},"PeriodicalIF":1.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13041630/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147589285","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

X-ray analysis of complexes of carbonic anhydrase II with 1,3-oxazole-containing sulfonamide derivatives elucidates the structural basis for their exceptionally high inhibitory potency 碳酸酐酶II与含1,3-恶唑的磺胺衍生物的配合物的x射线分析阐明了其异常高抑制效力的结构基础。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-01 Epub Date: 2026-03-23 DOI: 10.1107/S2053230X26002128

M. Y. Stoliarskaia, S. S. Borisevich, E. O. Myaskov, A. A. Shetnev, M. K. Korsakov, O. S. Nikonov

{"title":"X-ray analysis of complexes of carbonic anhydrase II with 1,3-oxazole-containing sulfonamide derivatives elucidates the structural basis for their exceptionally high inhibitory potency","authors":"M. Y. Stoliarskaia, S. S. Borisevich, E. O. Myaskov, A. A. Shetnev, M. K. Korsakov, O. S. Nikonov","doi":"10.1107/S2053230X26002128","DOIUrl":"10.1107/S2053230X26002128","url":null,"abstract":"Carbonic anhydrase II (CA2) is a zinc metalloenzyme that catalyzes the reversible hydration of CO2 and is widely used as a model for structure-guided inhibitor development. Previously reported crystal structures of human CA II (α-hCA2) in complex with the picomolar sulfonamide inhibitors 8V5 and 8V8 (PDB entries 5nee and 5nea) did not allow the complete ligand geometry of 8V5 to be resolved. To clarify the structural basis of binding, we determined high-resolution (1.5–1.7 Å) crystal structures of bovine CA II (α-bCA2) in complex with both inhibitors. α-bCA2 was selected as a crystallographically robust homolog, and structural alignment with α-hCA2 showed an r.m.s.d. of <0.44 Å across Cα atoms, confirming a near-identical active-site architecture. The α-bCA2–8V8 complex reproduced the canonical sulfonamide–zinc coordination pattern. In contrast, the α-bCA2–8V5 structure revealed continuous electron density for the entire ligand, including the morpholine group, which was not observed previously. Re-refinement of the α-hCA2–8V5 model based on these data resulted in an improved fit to density, indicating that the absence of the morpholine density in the original model is consistent with partial ligand modification or variability in the ligand state during crystallization. These results demonstrate that cross-isoform structural comparison can resolve ambiguities in ligand modeling and provide a reliable framework for the rational design of selective CA2 inhibitors.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 4","pages":"125-135"},"PeriodicalIF":1.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147462548","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}

引用次数: 0

Crystallization and 1.6 Å resolution crystal structure of an acylated GLP-1/GIP analogue peptide. 酰化GLP-1/GIP类似物肽的结晶和1.6 Å分辨率晶体结构。

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-01 Epub Date: 2026-03-17 DOI: 10.1107/S2053230X26001937

Hamish M Mitchell, Boguslaw Nocek, Emily J Guinn, Jerry Y Y Heng

{"title":"Crystallization and 1.6 Å resolution crystal structure of an acylated GLP-1/GIP analogue peptide.","authors":"Hamish M Mitchell, Boguslaw Nocek, Emily J Guinn, Jerry Y Y Heng","doi":"10.1107/S2053230X26001937","DOIUrl":"10.1107/S2053230X26001937","url":null,"abstract":"With the meteoric rise in interest in GLP-1 and GIP analogue peptides in recent years, there is a drive for the use of alternative purification techniques to alleviate processing bottlenecks and reduce the cost of peptide manufacturing. However, a lack of reported crystal structures for this class of peptides has hindered molecular-scale understanding of GLP-1/GIP analogue peptide crystallization, particularly related to acylated peptides. This paper therefore reports what is believed to be the first crystal structure of a GLP-1 and GIP analogue lipopeptide. Crystals obtained using a microseed matrix-screening protocol diffracted to ≤1.6 Å resolution in space group P43, with unit-cell parameters a = b = 64.66, c = 11.42 Å. Model building and the resultant structural analysis reveals that the predominantly helical peptide forms a uniquely porous spiral crystal structure composed of clockwise-ascending monomers in a square pattern, with aromatic C...H-π interactions around Phe22 forming the primary crystal contact between neighbouring square motifs.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"114-124"},"PeriodicalIF":1.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13041627/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147466523","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 PM1Pgh, a poly-γ-glutamate hydrolase from Bacillus phage PM1 Bacillus噬菌体PM1聚γ-谷氨酸水解酶PM1Pgh的晶体结构

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-04-01 DOI: 10.1107/S2053230X26002189

Kyoko Abe, Kenji Fukui, Yasunori Ogura

{"title":"Crystal structure of PM1Pgh, a poly-γ-glutamate hydrolase from Bacillus phage PM1","authors":"Kyoko Abe, Kenji Fukui, Yasunori Ogura","doi":"10.1107/S2053230X26002189","DOIUrl":"10.1107/S2053230X26002189","url":null,"abstract":"Poly-γ-glutamate (γ-PGA) is the key biopolymer responsible for the characteristic viscosity of natto, a traditional Japanese food produced by Bacillus subtilis var. natto. Phage infection frequently leads to γ-PGA degradation and loss of viscosity, a longstanding problem in natto production. While the γ-PGA hydrolase PghP from phage ΦNIT1 has been well characterized, the homologous enzyme encoded by B. subtilis var. natto phage PM1 has remained unstudied and is currently annotated only as ORF34; this protein is referred to here as PM1Pgh. Two catalytic models have been proposed for γ-PGA-degrading metallopeptidases: a direct anhydride mechanism involving the catalytic glutamate and a zinc-dependent, water-mediated mechanism. However, no definitive structural evidence has been obtained to distinguish between these mechanisms. Here, recombinant PM1Pgh was shown to possess γ-PGA hydrolase activity in vitro, and its crystal structures were determined in both zinc-free and zinc-bound states. The zinc-bound structure revealed a Zn2+ ion specifically coordinated within the catalytic pocket together with a well ordered water molecule positioned for nucleophilic attack, supporting a zinc-dependent, water-mediated mechanism for γ-PGA hydrolysis, consistent with the canonical mechanism of metallopeptidases.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 4","pages":"136-142"},"PeriodicalIF":1.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147508572","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}

引用次数: 0

IF 1.1 4区生物学

Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-03-17

引用次数: 0