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1XNZ

Crystal Structure of Mn(II) form of E. coli. Methionine Aminopeptidase in complex with 5-(2-chlorophenyl)furan-2-carboxylic acid

Summary for 1XNZ
Entry DOI10.2210/pdb1xnz/pdb
Related2MAT
DescriptorMethionine aminopeptidase, MANGANESE (II) ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsmethionine aminopeptidase, complex, inhibitor, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight29726.33
Authors
Ye, Q.-Z.,Xie, S.-X.,Huang, M.,Huang, W.-J.,Lu, J.-P.,Ma, Z.-Q. (deposition date: 2004-10-05, release date: 2004-11-02, Last modification date: 2024-02-14)
Primary citationYe, Q.-Z.,Xie, S.-X.,Huang, M.,Huang, W.-J.,Lu, J.-P.,Ma, Z.-Q.
Metalloform-Selective Inhibitors of Escherichia coli Methionine Aminopeptidase and X-ray Structure of a Mn(II)-Form Enzyme Complexed with an Inhibitor.
J.Am.Chem.Soc., 126:13940-13941, 2004
Cited by
PubMed Abstract: Methionine aminopeptidase (MetAP) enzymes require a divalent metal ion such as Mn(II), Fe(II), Co(II), Ni(II), or Zn(II) for its removal of the N-terminal methionine from newly synthesized proteins, but it is not certain which of these ions is most important in vivo. Metalloform-selective MetAP inhibitors could be valuable for defining which metals are physiologically relevant for MetAP activation and could serve as leads for development of new therapeutic agents. We have screened a library of 43 736 small drug-like molecules against Escherichia coli MetAP and identified two groups of potent and highly metalloform-selective inhibitors of the Co(II)-form, and of the Mn(II)-form, of this enzyme. Compound 1 is 790-fold more selective for the Co(II)-form, while compound 4 is over 640-fold more potent toward the Mn(II)-form. The X-ray structure of a di-Mn(II) form of E. coli MetAP complexed with the Mn(II)-form-selective compound 4 was obtained, and it shows that the inhibitor interacts with both Mn(II) ions through the two oxygen atoms of its free carboxylate group. The preferential coordination of the hard (oxygen) donors to Mn(II) may contribute to its superb selectivity toward the Mn(II)-form.
PubMed: 15506752
DOI: 10.1021/ja045864p
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.52 Å)
Structure validation

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数据于2025-07-09公开中

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