2F8H

Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form

Summary for 2F8H

• Entry DOI: 10.2210/pdb2f8h/pdb
• Related: 1YH1 2F7V
• Descriptor: aectylcitrulline deacetylase (2 entities in total)
• Functional Keywords: alpha/beta, hydrolase
• Biological source: Xanthomonas campestris
• Total number of polymer chains: 1
• Total formula weight: 39165.89

Authors

Shi, D.,Yu, X.,Roth, L.,Allewell, N.M.,Tuchman, M. (deposition date: 2005-12-02, release date: 2006-09-26, Last modification date: 2023-08-30)

Primary citation

Shi, D.,Yu, X.,Roth, L.,Tuchman, M.,Allewell, N.M.
Structure of a novel N-acetyl-L-citrulline deacetylase from Xanthomonas campestris
Biophys.Chem., 126:86-93, 2007

PubMed Abstract: 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.

PubMed: 16750290
DOI: 10.1016/j.bpc.2006.05.013

Experimental method

X-RAY DIFFRACTION (1.75 Å)