2f8h

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{{Seed}}
 
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[[Image:2f8h.png|left|200px]]
 
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==Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form==
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The line below this paragraph, containing "STRUCTURE_2f8h", creates the "Structure Box" on the page.
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<StructureSection load='2f8h' size='340' side='right'caption='[[2f8h]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_2f8h| PDB=2f8h | SCENE= }}
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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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===Structure of acetylcitrulline deacetylase from Xanthomonas campestris in metal-free form===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16750290}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2f8h" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16750290 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16750290}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2F8H is a 1 chain 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].
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==Reference==
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<ref group="xtra">PMID:16750290</ref><references group="xtra"/>
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[[Category: Acetylornithine deacetylase]]
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[[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 Mon Feb 16 12:10:14 2009''
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Current revision

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

PDB ID 2f8h

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