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The structure of Mlc titration factor a (MtfA/YeeI) reveals a prototypical zinc metallopeptidase related to anthrax lethal factor

Academic Article
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Overview

authors

  • Xu, Q. P.
  • 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, Scott
  • Jahreis, K.
  • Wilson, Ian

publication date

  • June 2012

journal

  • Journal of Bacteriology  Journal

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).

subject areas

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Antigens, Bacterial
  • Bacterial Proteins
  • Bacterial Toxins
  • Catalytic Domain
  • Crystallography, X-Ray
  • Klebsiella pneumoniae
  • Metalloendopeptidases
  • Metalloproteases
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Sequence Alignment
  • Zinc
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Identity

PubMed Central ID

  • PMC3370624

International Standard Serial Number (ISSN)

  • 0021-9193

Digital Object Identifier (DOI)

  • 10.1128/jb.00038-12

PubMed ID

  • 22467785
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Additional Document Info

start page

  • 2987

end page

  • 2999

volume

  • 194

issue

  • 11

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