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

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IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-03-17
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 4","pages":"114-124"},"PeriodicalIF":1.1,"publicationDate":"2026-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147708312","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
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 4","pages":"114-124"},"PeriodicalIF":1.1,"publicationDate":"2026-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147668620","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
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 4","pages":"143-149"},"PeriodicalIF":1.1,"publicationDate":"2026-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147668621","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 : 2026-03-05
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 3","pages":"94-100"},"PeriodicalIF":1.1,"publicationDate":"2026-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147563386","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 X-ray structure of a highly aggregation-prone monobody engineered for high-affinity small-molecule recognition 用于高亲和力小分子识别的高聚集倾向单体的结晶和x射线结构。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-03-05 Epub Date: 2026-03-03 DOI: 10.1107/S2053230X26000798
Koushirou Endo, Shun Umemoto, Nariaki Tsuzuki, Hideo Okumura, Yusuke Sato, Tatsuyuki Yoshii, Shinya Tsukiji, Shingo Nagano, Hiroshi Murakami, Tomoya Hino
{"title":"Crystallization and X-ray structure of a highly aggregation-prone monobody engineered for high-affinity small-molecule recognition","authors":"Koushirou Endo,&nbsp;Shun Umemoto,&nbsp;Nariaki Tsuzuki,&nbsp;Hideo Okumura,&nbsp;Yusuke Sato,&nbsp;Tatsuyuki Yoshii,&nbsp;Shinya Tsukiji,&nbsp;Shingo Nagano,&nbsp;Hiroshi Murakami,&nbsp;Tomoya Hino","doi":"10.1107/S2053230X26000798","DOIUrl":"10.1107/S2053230X26000798","url":null,"abstract":"<p>Monobodies, engineered protein scaffolds derived from the fibronectin type III domain, are powerful alternatives to conventional antibodies. While the native scaffold is robust, engineering the variable loops can often compromise solubility and promote aggregation. Here, we report the crystallization and structure determination at 2.57 Å resolution of a monobody (Mb-P′) engineered to bind the synthetic small molecule HPPU [1-(4-hydroxyphenyl)-3-phenylurea] with nanomolar affinity. Although Mb-P′ exhibited severe polydispersity and heterogeneous oligomerization in solution, N-terminal fusion with maltose-binding protein (MBP) using an optimized linker successfully yielded monodisperse species and diffraction-quality crystals. The crystal structure exhibited pseudo-<i>D</i><sub>3</sub> symmetry in the asymmetric unit, in which the MBP moiety interacts with and partially covers the F and G β-strands of the monobody. This steric masking suggests that MBP acts as a solubility enhancer by shielding the aggregation-prone surface patches generated by loop engineering. Our results demonstrate that this fusion strategy effectively enables structural studies of aggregation-prone proteins obtained from engineered scaffolds.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 3","pages":"75-82"},"PeriodicalIF":1.1,"publicationDate":"2026-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146140667","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 : 2026-03-05
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 3","pages":"83-93"},"PeriodicalIF":1.1,"publicationDate":"2026-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147563385","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 : 2026-03-03
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 3","pages":"66-74"},"PeriodicalIF":1.1,"publicationDate":"2026-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147563009","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
Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain. MexY -MexY嵌合外排泵的低温电镜结构揭示了MexY波特域固有的大开放裂缝。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-03-01 Epub Date: 2026-02-26 DOI: 10.1107/S2053230X26001202
Jiye Wang, Kenta Tsutsumi, Mika Hirose, Ryosuke Nakashima, Takayuki Kato, Kunihiko Nishino, Atsushi Nakagawa, Eiki Yamashita
{"title":"Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain.","authors":"Jiye Wang, Kenta Tsutsumi, Mika Hirose, Ryosuke Nakashima, Takayuki Kato, Kunihiko Nishino, Atsushi Nakagawa, Eiki Yamashita","doi":"10.1107/S2053230X26001202","DOIUrl":"10.1107/S2053230X26001202","url":null,"abstract":"<p><p>RND-type multidrug-efflux pumps are major contributors to multidrug resistance in Gram-negative bacteria, with MexY from Pseudomonas aeruginosa playing a central role in aminoglycoside resistance. Unlike other RND transporters, MexY exhibits unusually large open clefts in the binding and extrusion states. To determine whether this feature is intrinsic to its drug-recognition porter domain, we created a chimeric protein, MexBYB, by replacing the funnel-like and transmembrane domains of MexY with those of the homologous transporter MexB, and determined its structures by cryoEM under apo and kanamycin-supplemented conditions. Under both conditions, MexBYB was reported to adopt symmetric-like and asymmetric conformations. Structural comparisons reveal that the unusually large open clefts are retained in MexBYB, indicating that this feature is intrinsic to the MexY porter domain.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"83-93"},"PeriodicalIF":1.1,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12961675/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147289092","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 carbon-nitrogen hydrolase from Helicobacter pylori G27. 幽门螺杆菌G27碳氮水解酶的晶体结构。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-03-01 Epub Date: 2026-02-18 DOI: 10.1107/S2053230X26001330
Aruesha Srivastava, Jesuferanmi P Ayanlade, Lema Suleiman, Hannah Udell, Jan Abendroth, Donald J Lorimer, Thomas E Edwards, Bart L Staker, Rachael Zigweid, Sandhya Subramanian, Peter J Myler, Graham Chakafana, Oluwatoyin A Asojo
{"title":"Crystal structure of carbon-nitrogen hydrolase from Helicobacter pylori G27.","authors":"Aruesha Srivastava, Jesuferanmi P Ayanlade, Lema Suleiman, Hannah Udell, Jan Abendroth, Donald J Lorimer, Thomas E Edwards, Bart L Staker, Rachael Zigweid, Sandhya Subramanian, Peter J Myler, Graham Chakafana, Oluwatoyin A Asojo","doi":"10.1107/S2053230X26001330","DOIUrl":"10.1107/S2053230X26001330","url":null,"abstract":"<p><p>Carbon-nitrogen hydrolases (CNHs) are members of the diverse nitrilase superfamily of enzymes that facilitate cellular adaptation to environmental stress by metabolizing nitrogen, detoxifying xenobiotics and catabolizing environmentally derived metabolites. Helicobacter pylori CNH (HpCNH) may contribute to metabolic flexibility under acid stress, detoxification of reactive nitrogen species or nutrient scavenging in the nutrient-limited gastric environment. Here, we report the 2.1 Å resolution crystal structure of a CNH from H. pylori strain G27 (PDB entry 6mg6). HpCNH adopts the characteristic nitrilase-superfamily αββα-sandwich core and contains the conserved catalytic cysteine typical of enzymatically active CNHs. The overall structure and active site of HpCNH are most similar to those of carbamoylputrescine amidohydrolase from the plant Medicago truncatula. Despite structural variations in loop regions, including near the active site, HpCNH retains the key residues required to bind putrescine and the prototypical N-carbamoylputrescine amidase active site.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"66-74"},"PeriodicalIF":1.1,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12961655/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146218261","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 endo-β-N-acetylglucosaminidase HSα. 内切β- n -乙酰氨基葡萄糖酶HSα的晶体结构。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2026-03-01 Epub Date: 2026-02-28 DOI: 10.1107/S2053230X26001214
Ikuya Kurauchi, Kazuki Okura, Chie Hosokawa, Kazuo Ito, Ikuko Miyahara
{"title":"Crystal structure of endo-β-N-acetylglucosaminidase HSα.","authors":"Ikuya Kurauchi, Kazuki Okura, Chie Hosokawa, Kazuo Ito, Ikuko Miyahara","doi":"10.1107/S2053230X26001214","DOIUrl":"10.1107/S2053230X26001214","url":null,"abstract":"<p><p>The crystal structure of endo-β-N-acetylglucosaminidase HSα (Endo HSα) was determined at 1.8 Å resolution, revealing that the enzyme is composed of five distinct domains. Domains I to III adopt a fold that is conserved among GH85 enzymes, with catalytic residues Asn216, Glu218 and Tyr252 corresponding to conserved positions, while Tyr282 is newly implicated in catalysis based on the Endo HSα structure. A long loop unique to Endo HSα constricts the active site in domain I. Domain IV represents a novel structural element that is not observed in other GH85 enzymes. Its glycan-binding model and structural similarity to known sugar-binding domains play a role in substrate recognition. The minimal contacts with other domains allow it to remain flexible, accommodating bulky substrates at the active site. These features provide insights into the structural basis for substrate specificity and expand the structural diversity of the GH85 family.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"82 Pt 3","pages":"94-100"},"PeriodicalIF":1.1,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12961652/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147353417","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
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