2f7v: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='2f7v' size='340' side='right'caption='[[2f7v]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='2f7v' size='340' side='right'caption='[[2f7v]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2f7v]] is a 1 chain structure with sequence from [https://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=2F7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F7V FirstGlance]. <br>
<table><tr><td colspan='2'>[[2f7v]] 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=2F7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F7V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></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]] 1.75&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yh1|1yh1]], [[2f8h|2f8h]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylornithine_deacetylase Acetylornithine deacetylase], with EC number [https://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=2f7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7v OCA], [https://pdbe.org/2f7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f7v RCSB], [https://www.ebi.ac.uk/pdbsum/2f7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f7v ProSAT]</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=2f7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7v OCA], [https://pdbe.org/2f7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f7v RCSB], [https://www.ebi.ac.uk/pdbsum/2f7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f7v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACDAS_XANCP ACDAS_XANCP] Catalyzes the deacetylation of N-acetyl-L-citrulline to produce L-citrulline. This is a step in an alternative arginine biosynthesis pathway (PubMed:16585758, PubMed:16511126). Is also able to catalyze the deacetylation of N-acetylornithine in vitro, with almost equal velocity. However, this reaction may be not relevant in vivo since Xanthomonas does not possess the canonical argF gene and cannot convert ornithine to citrulline via ArgF' (PubMed:16585758).<ref>PMID:16511126</ref> <ref>PMID:16585758</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f7v ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f7v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:16750290</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2f7v" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__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]]
Retrieved from "https://proteopedia.org/2f7v"