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Title: Structure of a Novel N-acetyl-L-citrulline Deacetylase from Xanthomonas campestris

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 {angstrom} 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 confirmation. 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 ofmore » the acetyl group.« less

Authors:
; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930367
Report Number(s):
BNL-81087-2008-JA
Journal ID: ISSN 0301-4622; BICIAZ; TRN: US200904%%655
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biophysical Chemistry; Journal Volume: 126
Country of Publication:
United States
Language:
English
Subject:
08 HYDROGEN; 36 MATERIALS SCIENCE; CARBONYLS; CARBOXYPEPTIDASES; CATALYSTS; CRYSTAL STRUCTURE; DIMERIZATION; DIMERS; ENZYMES; HYDROGEN; MONOMERS; PATHOGENS; POLYPEPTIDES; PROTEINS; PSEUDOMONAS; RESOLUTION; SIMULATION; SUBSTRATES; SYMMETRY; national synchrotron light source

Citation Formats

Shi,D., Yu, X., Roth, L., Tuchman, M., and Allewell, N. Structure of a Novel N-acetyl-L-citrulline Deacetylase from Xanthomonas campestris. United States: N. p., 2007. Web. doi:10.1016/j.bpc.2006.05.013.
Shi,D., Yu, X., Roth, L., Tuchman, M., & Allewell, N. Structure of a Novel N-acetyl-L-citrulline Deacetylase from Xanthomonas campestris. United States. doi:10.1016/j.bpc.2006.05.013.
Shi,D., Yu, X., Roth, L., Tuchman, M., and Allewell, N. Mon . "Structure of a Novel N-acetyl-L-citrulline Deacetylase from Xanthomonas campestris". United States. doi:10.1016/j.bpc.2006.05.013.
@article{osti_930367,
title = {Structure of a Novel N-acetyl-L-citrulline Deacetylase from Xanthomonas campestris},
author = {Shi,D. and Yu, X. and Roth, L. and Tuchman, M. and Allewell, N.},
abstractNote = {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 {angstrom} 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 confirmation. 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.},
doi = {10.1016/j.bpc.2006.05.013},
journal = {Biophysical Chemistry},
number = ,
volume = 126,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}