2ghr

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[[Image:2ghr.gif|left|200px]]<br /><applet load="2ghr" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ghr, resolution 2.400&Aring;" />
 
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'''Crystal structure of homoserine o-succinyltransferase (NP_981826.1) from Bacillus cereus ATCC 10987 at 2.40 A resolution'''<br />
 
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==About this Structure==
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==Crystal structure of homoserine o-succinyltransferase (NP_981826.1) from Bacillus cereus ATCC 10987 at 2.40 A resolution==
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2GHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Homoserine_O-succinyltransferase Homoserine O-succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.46 2.3.1.46] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHR OCA].
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<StructureSection load='2ghr' size='340' side='right'caption='[[2ghr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==Reference==
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<table><tr><td colspan='2'>[[2ghr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GHR FirstGlance]. <br>
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Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 A resolution., Zubieta C, Krishna SS, McMullan D, Miller MD, Abdubek P, Agarwalla S, Ambing E, Astakhova T, Axelrod HL, Carlton D, Chiu HJ, Clayton T, Deller M, DiDonato M, Duan L, Elsliger MA, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Kumar A, Marciano D, Morse AT, Nigoghossian E, Oommachen S, Reyes R, Rife CL, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA, Proteins. 2007 Sep 1;68(4):999-1005. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17546672 17546672]
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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]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2ghr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ghr OCA], [https://pdbe.org/2ghr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ghr RCSB], [https://www.ebi.ac.uk/pdbsum/2ghr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ghr ProSAT], [https://www.topsan.org/Proteins/JCSG/2ghr TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/METAA_BACC1 METAA_BACC1] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine. Cannot use succinyl-CoA as the acyl donor.<ref>PMID:18216013</ref>
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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/gh/2ghr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ghr ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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[[Category: Homoserine O-succinyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: JCSG, Joint.Center.for.Structural.Genomics.]]
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[[Category: SO4]]
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[[Category: homoserine o-succinyltransferase]]
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[[Category: jcsg]]
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[[Category: joint center for structural genomics]]
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[[Category: np_981826.1]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:48:53 2008''
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Current revision

Crystal structure of homoserine o-succinyltransferase (NP_981826.1) from Bacillus cereus ATCC 10987 at 2.40 A resolution

PDB ID 2ghr

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