2pl5

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==Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans==
==Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans==
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<StructureSection load='2pl5' size='340' side='right' caption='[[2pl5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='2pl5' size='340' side='right'caption='[[2pl5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2pl5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"leptospira_icteroides"_noguchi_1919 "leptospira icteroides" noguchi 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PL5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2pl5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_interrogans Leptospira interrogans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PL5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=173 "Leptospira icteroides" Noguchi 1919])</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=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </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=2pl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pl5 OCA], [https://pdbe.org/2pl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pl5 RCSB], [https://www.ebi.ac.uk/pdbsum/2pl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pl5 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pl5 OCA], [http://pdbe.org/2pl5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pl5 RCSB], [http://www.ebi.ac.uk/pdbsum/2pl5 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/METX_LEPIN METX_LEPIN]] Involved in the methionine biosynthesis. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-homoserine to yield O-acetyl-L-homoserine.<ref>PMID:17927957</ref>
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[https://www.uniprot.org/uniprot/METXA_LEPIN METXA_LEPIN] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine (PubMed:17927957, PubMed:28581482). 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 (PubMed:17927957).<ref>PMID:17927957</ref> <ref>PMID:28581482</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/pl/2pl5_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pl/2pl5_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>
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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=2pl5 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=2pl5 ConSurf].
<div style="clear:both"></div>
<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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Homoserine O-acetyltransferase (HTA, EC 2.3.1.31) initiates methionine biosynthesis pathway by catalyzing the transfer of acetyl group from acetyl-CoA to homoserine. This study reports the crystal structure of HTA from Leptospira interrogans determined at 2.2A resolution using selenomethionyl single-wavelength anomalous diffraction method. HTA is modular and consists of two structurally distinct domains--a core alpha/beta domain containing the catalytic site and a helical bundle called the lid domain. Overall, the structure fold belongs to alpha/beta hydrolase superfamily with the characteristic 'catalytic triad' residues in the active site. Detailed structure analysis showed that the catalytic histidine and serine are both present in two conformations, which may be involved in the catalytic mechanism for acetyl transfer.
 
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Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans.,Wang M, Liu L, Wang Y, Wei Z, Zhang P, Li Y, Jiang X, Xu H, Gong W Biochem Biophys Res Commun. 2007 Nov 30;363(4):1050-6. Epub 2007 Sep 4. PMID:17927957<ref>PMID:17927957</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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<div class="pdbe-citations 2pl5" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Leptospira icteroides noguchi 1919]]
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[[Category: Large Structures]]
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[[Category: Homoserine O-acetyltransferase]]
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[[Category: Leptospira interrogans]]
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[[Category: Gong, W]]
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[[Category: Gong W]]
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[[Category: Liu, L]]
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[[Category: Liu L]]
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[[Category: Wang, M]]
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[[Category: Wang M]]
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[[Category: Wang, Y]]
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[[Category: Wang Y]]
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[[Category: Wei, Z]]
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[[Category: Wei Z]]
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[[Category: Xu, H]]
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[[Category: Xu H]]
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[[Category: Alpha/beta hydrolase superfamily]]
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[[Category: Homoserine o-acetyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans

PDB ID 2pl5

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