2pl5

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[[Image:2pl5.jpg|left|200px]]<br /><applet load="2pl5" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pl5, resolution 2.200&Aring;" />
 
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'''Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans'''<br />
 
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==Overview==
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==Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans==
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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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<StructureSection load='2pl5' size='340' side='right'caption='[[2pl5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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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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2PL5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leptospira_interrogans Leptospira interrogans] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PL5 OCA].
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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='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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==Reference==
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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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17927957 17927957]
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</table>
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[[Category: Homoserine O-acetyltransferase]]
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== Function ==
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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>
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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/pl/2pl5_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=2pl5 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>
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[[Category: Large Structures]]
[[Category: Leptospira interrogans]]
[[Category: Leptospira interrogans]]
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[[Category: Single protein]]
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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: GOL]]
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[[Category: alpha/beta hydrolase superfamily]]
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[[Category: homoserine o-acetyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:36 2008''
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Current revision

Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans

PDB ID 2pl5

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