2f8h
From Proteopedia
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| - | [[Image:2f8h.gif|left|200px]] | + | [[Image:2f8h.gif|left|200px]] |
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| - | '''Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form''' | + | {{Structure |
| + | |PDB= 2f8h |SIZE=350|CAPTION= <scene name='initialview01'>2f8h</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F8H is a [ | + | 2F8H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F8H OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16750290 16750290] |
[[Category: Acetylornithine deacetylase]] | [[Category: Acetylornithine deacetylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta]] | [[Category: alpha/beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:49:21 2008'' |
Revision as of 14:49, 20 March 2008
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| , resolution 1.75Å | |||||||
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| Activity: | Acetylornithine deacetylase, with EC number 3.5.1.16 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form
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
2F8H 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 Thu Mar 20 16:49:21 2008
