2f7v

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[[Image:2f7v.gif|left|200px]]
[[Image:2f7v.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2f7v |SIZE=350|CAPTION= <scene name='initialview01'>2f7v</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_2f7v", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylornithine_deacetylase Acetylornithine deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.16 3.5.1.16] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2f7v| PDB=2f7v | SCENE= }}
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|RELATEDENTRY=[[1yh1|1YH1]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7v OCA], [http://www.ebi.ac.uk/pdbsum/2f7v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f7v RCSB]</span>
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}}
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'''Structure of acetylcitrulline deacetylase complexed with one Co'''
'''Structure of acetylcitrulline deacetylase complexed with one Co'''
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[[Category: Tuchman, M.]]
[[Category: Tuchman, M.]]
[[Category: Yu, X.]]
[[Category: Yu, X.]]
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[[Category: alpha/beta]]
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[[Category: Alpha/beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:33:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:59:06 2008''
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Revision as of 00:33, 4 May 2008

Image:2f7v.gif

Template:STRUCTURE 2f7v

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. 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 Sun May 4 03:33:55 2008

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