Jose Malanho da Silva, Jose Lanuza, Francesco Bruno, Vito Calderone, Enrico Ravera
{"title":"The structure of His15 acetamide-modified hen egg-white lysozyme: a nice surprise from an old friend.","authors":"Jose Malanho da Silva, Jose Lanuza, Francesco Bruno, Vito Calderone, Enrico Ravera","doi":"10.1107/S2053230X2500010X","DOIUrl":"10.1107/S2053230X2500010X","url":null,"abstract":"<p><p>Hen egg-white lysozyme (HEWL) is a small polycationic protein which is highly soluble and stable. This has led to it becoming a `molecular laboratory' where chemical biological operations and structural techniques are tested. To date, HEWL accounts for 1233 PDB entries, roughly 0.5% of the total, making it the best-represented protein in the PDB. With the aim of unambiguously identifying the N atom of the His15 side chain that is most reactive towards iodoacetamide, the structure of chemically modified HEWL was determined by crystallizing it using the `15 minutes lysozyme' protocol. This protocol invariably yields tetragonal crystals of the unmodified protein. To our surprise, we found that the crystals of the modified protein had similar unit-cell parameters but that refinement was only possible when considering an orthorhombic system.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"41-46"},"PeriodicalIF":1.1,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11783178/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142968938","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}
{"title":"Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.","authors":"Michael R Rankin, Janet L Smith","doi":"10.1107/S2053230X25000068","DOIUrl":"10.1107/S2053230X25000068","url":null,"abstract":"<p><p>X-ray crystallography remains the dominant method of determining the three-dimensional structure of proteins. Nevertheless, this resource-intensive process may be hindered by the unintended crystallization of contaminant proteins from the expression source. Here, the serendipitous discovery of two novel crystal forms and one new, high-resolution structure of carbonic anhydrase 2 (CA2) from Escherichia coli that arose during a crystallization campaign for an unrelated target is reported. By comparing unit-cell parameters with those in the PDB, contaminants such as CA2 can be identified, preventing futile molecular-replacement attempts. Crystallographers can use these new lattice parameters to diagnose CA2 contamination in similar experiments.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"47-52"},"PeriodicalIF":1.1,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11783180/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142982328","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}
{"title":"CryoCrane: an open-source GUI for analyzing cryo-EM screening data sets.","authors":"Jakob Ruickoldt, Petra Wendler","doi":"10.1107/S2053230X25000081","DOIUrl":"10.1107/S2053230X25000081","url":null,"abstract":"<p><p>Screening of cryo-EM samples is essential for the generation of high-resolution cryo-EM structures. Often, it is cumbersome to correlate the appearance of specific grid squares and micrograph quality. Here, CryoCrane (Correlate atlas and exposures), a visualization tool for cryo-EM screening data, is presented. It aims to provide an intuitive way to visualize micrographs and to speed up data analysis.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"62-65"},"PeriodicalIF":1.1,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11783181/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142968756","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}
{"title":"Structural insights into the role of the prosegment binding loop in a papain-superfamily cysteine protease from Treponema denticola","authors":"N. D. Clark, C. Li, M. G. Malkowski","doi":"10.1107/S2053230X25000378","DOIUrl":"10.1107/S2053230X25000378","url":null,"abstract":"<p>Periodontal diseases afflict 20–50% of the global population and carry serious health and economic burdens. Chronic periodontitis is characterized by inflammation of the periodontal pocket caused by dysbiosis. This dysbiosis is coupled with an increase in the population of <i>Treponema denticola</i>, a spirochete bacterium with high mobility and invasivity mediated by a number of virulence factors. One such virulence factor is TDE0362, a multidomain protein with a carboxy-terminal papain-superfamily cysteine protease (C0362). Most papain-superfamily cysteine proteases are produced as proenzymes with a prodomain that interacts with the prosegment binding loop (PBL), requiring proteolytic processing for full activation. Previous studies have indicated that C0362 is not produced as a proenzyme, suggesting an alternative regulatory mechanism. We previously determined the crystal structure of C0362 captured in an inactive conformation with an oxidized catalytic cysteine and a disordered PBL. In this follow-up study, we evaluated the active-site architecture and the PBL in two mutant (Y559A and C412S) structures and an inhibitor-bound (E64) structure to provide insight into the role that the PBL plays in the generation of active enzyme. Our results implicate Tyr559 as playing a critical role in the transition of the enzyme to an active state. We subsequently utilized the structural information to generate models of C0362 bound to human complement factors C3 and C4. Collectively, our results provide insight into the regulatory mechanism and putative substrate-binding interfaces of C0362, highlighting avenues of further research towards inhibition of this essential virulence factor.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"81 2","pages":"53-61"},"PeriodicalIF":1.1,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143021740","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}