2pl5

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[[Image:2pl5.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans==
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|PDB= 2pl5 |SIZE=350|CAPTION= <scene name='initialview01'>2pl5</scene>, resolution 2.200&Aring;
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<StructureSection load='2pl5' size='340' side='right'caption='[[2pl5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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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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|ACTIVITY= <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>
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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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|GENE= metX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=173 Leptospira interrogans])
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2pl5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pl5 RCSB]</span>
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== Function ==
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}}
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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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'''Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans'''
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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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==Overview==
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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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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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<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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==About this Structure==
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</jmolCheckbox>
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2PL5 is a [[Single protein]] structure of sequence from [http://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].
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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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==Reference==
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== References ==
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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://www.ncbi.nlm.nih.gov/pubmed/17927957 17927957]
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<references/>
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[[Category: Homoserine O-acetyltransferase]]
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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: 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 Mon Mar 31 04:37:27 2008''
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Current revision

Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans

PDB ID 2pl5

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