{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T20:01:29Z","timestamp":1787169689130,"version":"build-2736575974"},"reference-count":64,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2012,6,1]],"date-time":"2012-06-01T00:00:00Z","timestamp":1338508800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2012,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    MtfA of\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n                    (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\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Klebsiella pneumoniae<\/jats:named-content>\n                    and its complex with zinc (holoenzyme) at 2.2 and 1.95 \u00c5, respectively. MtfA contains a conserved H\n                    <jats:sup>149<\/jats:sup>\n                    E\n                    <jats:sup>150<\/jats:sup>\n                    XXH\n                    <jats:sup>153<\/jats:sup>\n                    +E\n                    <jats:sup>212<\/jats:sup>\n                    +Y\n                    <jats:sup>205<\/jats:sup>\n                    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\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Vibrio cholerae<\/jats:named-content>\n                    , 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).\n                  <\/jats:p>","DOI":"10.1128\/jb.00038-12","type":"journal-article","created":{"date-parts":[[2012,3,31]],"date-time":"2012-03-31T00:07:59Z","timestamp":1333152479000},"page":"2987-2999","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":14,"title":["The Structure of Mlc Titration Factor A (MtfA\/YeeI) Reveals a Prototypical Zinc Metallopeptidase Related to Anthrax Lethal Factor"],"prefix":"10.1128","volume":"194","author":[{"given":"Qingping","family":"Xu","sequence":"first","affiliation":[{"name":"Joint Center for Structural Genomics, SLAC National Accelerator Laboratory, Menlo Park, California, USA"},{"name":"Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California, 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