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| | <StructureSection load='2f8h' size='340' side='right'caption='[[2f8h]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='2f8h' size='340' side='right'caption='[[2f8h]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f8h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_campestris"_pammel_1895 "bacillus campestris" pammel 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F8H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2f8h]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F8H FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yh1|1yh1]], [[2f7v|2f7v]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f8h OCA], [https://pdbe.org/2f8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f8h RCSB], [https://www.ebi.ac.uk/pdbsum/2f8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f8h ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f8h OCA], [http://pdbe.org/2f8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f8h RCSB], [http://www.ebi.ac.uk/pdbsum/2f8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f8h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H2X6W0_XANC8 A0A0H2X6W0_XANC8] Catalyzes the deacetylation of N-acetyl-L-citrulline to produce L-citrulline. This is a step in an alternative arginine biosynthesis pathway.[HAMAP-Rule:MF_02236] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus campestris pammel 1895]] | |
| - | [[Category: Acetylornithine deacetylase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allewell, N M]] | + | [[Category: Xanthomonas campestris]] |
| - | [[Category: Roth, L]] | + | [[Category: Allewell NM]] |
| - | [[Category: Shi, D]] | + | [[Category: Roth L]] |
| - | [[Category: Tuchman, M]] | + | [[Category: Shi D]] |
| - | [[Category: Yu, X]] | + | [[Category: Tuchman M]] |
| - | [[Category: Alpha/beta]]
| + | [[Category: Yu X]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A0A0H2X6W0_XANC8 Catalyzes the deacetylation of N-acetyl-L-citrulline to produce L-citrulline. This is a step in an alternative arginine biosynthesis pathway.[HAMAP-Rule:MF_02236]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shi D, Yu X, Roth L, Tuchman M, Allewell NM. Structure of a novel N-acetyl-L-citrulline deacetylase from Xanthomonas campestris. Biophys Chem. 2007 Mar;126(1-3):86-93. Epub 2006 Jun 5. PMID:16750290 doi:10.1016/j.bpc.2006.05.013
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