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2h2w

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==Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution==
==Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution==
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<StructureSection load='2h2w' size='340' side='right' caption='[[2h2w]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
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<StructureSection load='2h2w' size='340' side='right'caption='[[2h2w]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2h2w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H2W FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2h2w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2W FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr>
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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]] 2.52&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=2h2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2w OCA], [https://pdbe.org/2h2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2w RCSB], [https://www.ebi.ac.uk/pdbsum/2h2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2w ProSAT], [https://www.topsan.org/Proteins/JCSG/2h2w TOPSAN]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h2w RCSB], [http://www.ebi.ac.uk/pdbsum/2h2w PDBsum], [http://www.topsan.org/Proteins/JCSG/2h2w TOPSAN]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/METAA_THEMA METAA_THEMA] 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. Has weak activity with succinyl-CoA as the acyl donor.<ref>PMID:16708165</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2w_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2w_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2h2w ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homoserine O-succinyltransferase]]
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[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: JCSG, Joint Center for Structural Genomics.]]
 
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[[Category: Homoserine o-succinyltransferase]]
 
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[[Category: Homoserine o-transsuccinylase]]
 
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[[Category: Ht]]
 
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[[Category: Jcsg]]
 
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[[Category: Joint center for structural genomic]]
 
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[[Category: Protein structure initiative]]
 
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[[Category: Psi]]
 
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[[Category: Structural genomic]]
 
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[[Category: Tm0881]]
 
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[[Category: Transferase]]
 

Current revision

Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution

PDB ID 2h2w

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