2f7v
From Proteopedia
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Structure of acetylcitrulline deacetylase complexed with one Co
Overview
The structure of a novel acetylcitrulline deacetylase from the plant, pathogen Xanthomonas campestris has been solved by multiple-wavelength, anomalous dispersion (MAD) using crystals grown from, selenomethionine-substituted protein and refined at 1.75 A resolution. The, asymmetric unit of the crystal contains one monomer consisting of two, domains, a catalytic domain and a dimerization domain. The catalytic, domain is able to bind a single Co(II) ion at the active site with no, change in conformation. The dimerization domain forms an interface between, two monomers related by a crystallographic two-fold symmetry axis. The, interface is maintained by hydrophobic interactions between helices and, hydrogen bonding between two beta strands that form a continuous beta, sheet across the dimer interface. Because the dimers are also related by, two-fold crystallographic axes, they pack together across the crystal via, the dimerization domain, suggesting that higher order oligomers may form, in solution. The polypeptide fold of the monomer is similar to the fold of, Pseudomonas sp. carboxypeptidase G2 and Neisseria meningitidis succinyl, diaminopimelate desuccinylase. Structural comparison among these enzymes, allowed modeling of substrate binding and suggests a possible catalytic, mechanism, in which Glu130 functions as a bifunctional general acid-base, catalyst and the metal ion polarizes the carbonyl of the acetyl group.
About this Structure
2F7V is a Single protein structure of sequence from Xanthomonas campestris with as ligand. Active as Acetylornithine deacetylase, with EC number 3.5.1.16 Full crystallographic information is available from OCA.
Reference
Structure of a novel N-acetyl-L-citrulline deacetylase from Xanthomonas campestris., Shi D, Yu X, Roth L, Tuchman M, Allewell NM, Biophys Chem. 2007 Mar;126(1-3):86-93. Epub 2006 Jun 5. PMID:16750290
Page seeded by OCA on Tue Jan 29 19:29:36 2008
