The Structure of Mlc Titration Factor A (MtfA/YeeI) Reveals a Prototypical Zinc Metallopeptidase Related to Anthrax Lethal Factor

DC FieldValueLanguage
dc.contributor.authorXu, Qingping
dc.contributor.authorGoehler, Anna-Katharina
dc.contributor.authorKosfeld, Anne
dc.contributor.authorCarlton, Dennis
dc.contributor.authorChiu, Hsiu-Ju
dc.contributor.authorKlock, Heath E.
dc.contributor.authorKnuth, Mark W.
dc.contributor.authorMiller, Mitchell D.
dc.contributor.authorElsliger, Marc-Andre
dc.contributor.authorDeacon, Ashley M.
dc.contributor.authorGodzik, Adam
dc.contributor.authorLesley, Scott A.
dc.contributor.authorJahreis, Knut
dc.contributor.authorWilson, Ian A.
dc.date.accessioned2021-12-23T16:23:29Z-
dc.date.available2021-12-23T16:23:29Z-
dc.date.issued2012
dc.identifier.issn00219193
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/14551-
dc.description.abstractMtfA of Escherichia coli (formerly YeeI) was previously identified as a regulator of the phosphoenolpyruvate (PEP)-dependent: glucose phosphotransferase system. MtfA homolog proteins are highly conserved, especially among beta- and gammaproteobacteria. We determined the crystal structures of the full-length MtfA apoenzyme from Klebsiella pneumoniae and its complex with zinc (holoenzyme) at 2.2 and 1.95 angstrom, respectively. MtfA contains a conserved (HEXXH153)-E-149-X-150+E-212+Y-205 metallopeptidase motif. The presence of zinc in the active site induces significant conformational changes in the region around Tyr205 compared to the conformation of the apoenzyme. Additionally, the zinc-bound MtfA structure is in a self-inhibitory conformation where a region that was disordered in the unliganded structure is now observed in the active site and a nonproductive state of the enzyme is formed. MtfA is related to the catalytic domain of the anthrax lethal factor and the Mop protein involved in the virulence of Vibrio cholerae, with conservation in both overall structure and in the residues around the active site. These results clearly provide support for MtfA as a prototypical zinc metallopeptidase (gluzincin clan).
dc.description.sponsorshipDOE Office of Biological and Environmental ResearchUnited States Department of Energy (DOE); National Institutes of Health, National Center for Research ResourcesUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Center for Research Resources (NCRR) [P41RR001209]; National Institute of General Medical SciencesUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS); NIH, National Institute of General Medical Sciences, Protein Structure InitiativeUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [U54 GM094586, GM074898]; German Federal Ministry of Education and ResearchFederal Ministry of Education & Research (BMBF) [FKZ 0315285C]; German Research FoundationGerman Research Foundation (DFG) [SFB431]; NATIONAL CENTER FOR RESEARCH RESOURCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Center for Research Resources (NCRR) [P41RR001209] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [U54GM094586, U54GM074898] Funding Source: NIH RePORTER; The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program (grant P41RR001209), and the National Institute of General Medical Sciences. This work was supported by the NIH, National Institute of General Medical Sciences, Protein Structure Initiative (grants U54 GM094586 and GM074898), the German Federal Ministry of Education and Research (grant FKZ 0315285C), and the German Research Foundation (grant SFB431).
dc.language.isoen
dc.publisherAMER SOC MICROBIOLOGY
dc.relation.ispartofJOURNAL OF BACTERIOLOGY
dc.subjectBACILLUS-ANTHRACIS
dc.subjectCRYSTAL-STRUCTURE
dc.subjectEPIDEMIC VIBRIO-CHOLERAE
dc.subjectESCHERICHIA-COLI K-12
dc.subjectGLUCOSE-PHOSPHOTRANSFERASE SYSTEM
dc.subjectHIGH-PATHOGENICITY ISLAND
dc.subjectMEMBRANE SEQUESTRATION
dc.subjectMicrobiology
dc.subjectPROTEIN
dc.subjectSECONDARY STRUCTURE
dc.subjectSTRUCTURE PREDICTION
dc.titleThe Structure of Mlc Titration Factor A (MtfA/YeeI) Reveals a Prototypical Zinc Metallopeptidase Related to Anthrax Lethal Factor
dc.typejournal article
dc.identifier.doi10.1128/JB.00038-12
dc.identifier.isiISI:000304227800022
dc.description.volume194
dc.description.issue11
dc.description.startpage2987
dc.description.endpage2999
dc.contributor.orcid0000-0002-2425-852X
dc.contributor.orcid0000-0002-2425-852X
dc.contributor.researcheridA-7279-2009
dc.contributor.researcheridAAW-1467-2020
dc.identifier.eissn10985530
dc.publisher.place1752 N ST NW, WASHINGTON, DC 20036-2904 USA
dcterms.isPartOf.abbreviationJ. Bacteriol.
dcterms.oaStatusGreen Published, Bronze
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