{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Prester A"],"funding":["Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research)","Bundesministerium für Bildung und Forschung","Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)","Joachim Herz Stiftung","Joachim Herz Stiftung (Joachim Herz Foundation)"],"pagination":["152"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11226702"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(1)"],"pubmed_abstract":["The emergence and spread of antibiotic resistance represent a growing threat to public health. Of particular concern is the appearance of β-lactamases, which are capable to hydrolyze and inactivate the most important class of antibiotics, the β-lactams. Effective β-lactamase inhibitors and mechanistic insights into their action are central in overcoming this type of resistance, and in this context boronate-based β-lactamase inhibitors were just recently approved to treat multidrug-resistant bacteria. Using boric acid as a simplified inhibitor model, time-resolved serial crystallography was employed to obtain mechanistic insights into binding to the active site serine of β-lactamase CTX-M-14, identifying a reaction time frame of 80-100 ms. In a next step, the subsequent 1,2-diol boric ester"],"journal":["Communications chemistry"],"pubmed_title":["Time-resolved crystallography of boric acid binding to the active site serine of the β-lactamase CTX-M-14 and subsequent 1,2-diol esterification."],"pmcid":["PMC11226702"],"funding_grant_id":["05K19GU4","05K20GUB","390715994","Infecto-physics"],"pubmed_authors":["Chapman H","Werner N","Aepfelbacher M","Rohde H","Hakanpaa J","Betzel C","Meyer J","Perbandt M","Henkel A","Hinrichs W","Oberthuer D","Yefanov O","Pompidor G","Maracke J","Prester A","Galchenkova M"],"additional_accession":[]},"is_claimable":false,"name":"Time-resolved crystallography of boric acid binding to the active site serine of the β-lactamase CTX-M-14 and subsequent 1,2-diol esterification.","description":"The emergence and spread of antibiotic resistance represent a growing threat to public health. Of particular concern is the appearance of β-lactamases, which are capable to hydrolyze and inactivate the most important class of antibiotics, the β-lactams. Effective β-lactamase inhibitors and mechanistic insights into their action are central in overcoming this type of resistance, and in this context boronate-based β-lactamase inhibitors were just recently approved to treat multidrug-resistant bacteria. Using boric acid as a simplified inhibitor model, time-resolved serial crystallography was employed to obtain mechanistic insights into binding to the active site serine of β-lactamase CTX-M-14, identifying a reaction time frame of 80-100 ms. In a next step, the subsequent 1,2-diol boric ester","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-05-29T09:39:35.481Z","creation":"2024-11-20T23:50:09.031Z"},"accession":"S-EPMC11226702","cross_references":{"pubmed":["38969718"],"doi":["10.1038/s42004-024-01236-w"]}}