2f8h

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(New page: 200px<br /><applet load="2f8h" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f8h, resolution 1.75&Aring;" /> '''Structure of acetylc...)
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[[Image:2f8h.gif|left|200px]]<br /><applet load="2f8h" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2f8h, resolution 1.75&Aring;" />
 
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'''Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form'''<br />
 
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==Overview==
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==Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form==
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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.
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<StructureSection load='2f8h' size='340' side='right'caption='[[2f8h]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f8/2f8h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2f8h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2F8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F8H OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16750290 16750290]
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</div>
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[[Category: Acetylornithine deacetylase]]
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<div class="pdbe-citations 2f8h" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Xanthomonas campestris]]
[[Category: Xanthomonas campestris]]
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[[Category: Allewell, N.M.]]
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[[Category: Allewell NM]]
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[[Category: Roth, L.]]
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[[Category: Roth L]]
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[[Category: Shi, D.]]
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[[Category: Shi D]]
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[[Category: Tuchman, M.]]
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[[Category: Tuchman M]]
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[[Category: Yu, X.]]
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[[Category: Yu X]]
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[[Category: alpha/beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:30:14 2008''
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Current revision

Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form

PDB ID 2f8h

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