3KHI

Crystal structure of a Putative Metal-dependent Hydrolase (YP_001336084.1) from Klebsiella pneumoniae subsp. pneumoniae MGH 78578 at 1.95 A resolution

Summary for 3KHI

• Entry DOI: 10.2210/pdb3khi/pdb
• Descriptor: Putative Metal-dependent Hydrolase, ZINC ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: a putative metal-dependent hydrolase, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, hydrolase
• Biological source: Klebsiella pneumoniae subsp. pneumoniae MGH 78578
• Total number of polymer chains: 1
• Total formula weight: 31120.28

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2009-10-30, release date: 2009-11-10, Last modification date: 2024-10-09)

Primary citation

Xu, Q.,Gohler, A.K.,Kosfeld, A.,Carlton, D.,Chiu, H.J.,Klock, H.E.,Knuth, M.W.,Miller, M.D.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Jahreis, K.,Wilson, I.A.
The Structure of Mlc Titration Factor A (MtfA/YeeI) Reveals a Prototypical Zinc Metallopeptidase Related to Anthrax Lethal Factor.
J.Bacteriol., 194:2987-2999, 2012

PubMed Abstract: MtfA 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 Å, respectively. MtfA contains a conserved H(149)E(150)XXH(153)+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).

PubMed: 22467785
DOI: 10.1128/JB.00038-12

Experimental method

X-RAY DIFFRACTION (1.95 Å)