{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T14:07:05Z","timestamp":1740146825344,"version":"3.37.3"},"reference-count":38,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2022,10,20]],"date-time":"2022-10-20T00:00:00Z","timestamp":1666224000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM124898"],"award-info":[{"award-number":["R35GM124898"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["HHSN272201700059C"],"award-info":[{"award-number":["HHSN272201700059C"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Institutes of Health, Department of Health and Human Services"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p><jats:italic>Klebsiella pneumoniae<\/jats:italic> is a bacterial pathogen that is increasingly responsible for hospital-acquired pneumonia and sepsis. Progressive development of antibiotic resistance has led to higher mortality rates and creates a need for novel treatments. Because of the essential role that nucleotides play in many bacterial processes, enzymes involved in purine and pyrimidine metabolism and transport are ideal targets for the development of novel antibiotics. Herein we describe the structure of <jats:italic>K<\/jats:italic>. <jats:italic>pneumoniae<\/jats:italic> adenosine monophosphate nucleosidase (KpAmn), a purine salvage enzyme unique to bacteria, as determined by cryoelectron microscopy. The data detail a well conserved fold with a hexameric overall structure and clear density for the putative active site residues. Comparison to the crystal structures of homologous prokaryotic proteins confirms the presence of many of the conserved structural features of this protein yet reveals differences in distal loops in the absence of crystal contacts. This first cryo-EM structure of an Amn enzyme provides a basis for future structure-guided drug development and extends the accuracy of structural characterization of this family of proteins beyond this clinically relevant organism.<\/jats:p>","DOI":"10.1371\/journal.pone.0275023","type":"journal-article","created":{"date-parts":[[2022,10,20]],"date-time":"2022-10-20T18:37:28Z","timestamp":1666291048000},"page":"e0275023","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structure of Klebsiella pneumoniae adenosine monophosphate nucleosidase"],"prefix":"10.1371","volume":"17","author":[{"given":"Brian C.","family":"Richardson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roger","family":"Shek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wesley C.","family":"Van Voorhis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6762-1309","authenticated-orcid":true,"given":"Jarrod B.","family":"French","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2022,10,20]]},"reference":[{"key":"pone.0275023.ref001","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1128\/MMBR.00078-15","article-title":"Klebsiella pneumoniae: Going on the Offense with a Strong Defense","volume":"80","author":"MK Paczosa","journal-title":"Microbiol Mol Biol Rev"},{"key":"pone.0275023.ref002","article-title":"Global Dissemination of Carbapenemase-Producing Klebsiella pneumoniae: Epidemiology, Genetic Context, Treatment Options, and Detection Methods","volume":"7","author":"C-R Lee","year":"2016","journal-title":"Front Microbiol"},{"key":"pone.0275023.ref003","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2019.00539","article-title":"Emerging Strategies to Combat ESKAPE Pathogens in the Era of Antimicrobial Resistance: A Review","volume":"10","author":"MS Mulani","year":"2019","journal-title":"Front Microbiol."},{"key":"pone.0275023.ref004","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.biotechadv.2018.11.013","article-title":"Antibiotic resistance in Pseudomonas aeruginosa: mechanisms and alternative therapeutic strategies","volume":"37","author":"Z Pang","year":"2019","journal-title":"Biotechnol Adv"},{"key":"pone.0275023.ref005","article-title":"Prevalence and Therapies of Antibiotic-Resistance in Staphylococcus aureus","volume":"10","author":"Y Guo","year":"2020","journal-title":"Front Cell Infect Microbiol"},{"key":"pone.0275023.ref006","doi-asserted-by":"crossref","first-page":"2730","DOI":"10.1073\/pnas.76.6.2730","article-title":"Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases","volume":"76","author":"RR Yocum","year":"1979","journal-title":"Proc Natl Acad Sci"},{"key":"pone.0275023.ref007","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/nrmicro1486","article-title":"Breaching the great wall: peptidoglycan and microbial interactions","volume":"4","author":"KA Cloud-Hansen","year":"2006","journal-title":"Nat Rev Microbiol"},{"key":"pone.0275023.ref008","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1111\/j.1432-1033.1968.tb19584.x","article-title":"The Puromycin Reaction and its Inhibition by Chloramphenicol","volume":"7","author":"M. 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