1i6w

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(New page: 200px<br /><applet load="1i6w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i6w, resolution 1.5&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1i6w.jpg|left|200px]]<br /><applet load="1i6w" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1i6w, resolution 1.5&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE: A MINIMAL ALPHA/BETA HYDROLASE ENZYME'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE: A MINIMAL ALPHA/BETA HYDROLASE ENZYME==
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The X-ray structure of the lipase LipA from Bacillus subtilis has been, determined at 1.5 A resolution. It is the first structure of a member of, homology family 1.4 of bacterial lipases. The lipase shows a compact, minimal alpha/beta hydrolase fold with a six-stranded parallel beta-sheet, flanked by five alpha-helices, two on one side of the sheet and three on, the other side. The catalytic triad residues, Ser77, Asp133 and His156, and the residues forming the oxyanion hole (backbone amide groups of Ile12, and Met78) are in positions very similar to those of other lipases of, known structure. However, no lid domain is present and the active-site, nucleophile Ser77 is solvent-exposed. A model of substrate binding is, proposed on the basis of a comparison with other lipases with a covalently, bound tetrahedral intermediate mimic. It explains the preference of the, enzyme for substrates with C8 fatty acid chains.
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<StructureSection load='1i6w' size='340' side='right'caption='[[1i6w]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i6w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6W FirstGlance]. <br>
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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]] 1.5&#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=CD:CADMIUM+ION'>CD</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=1i6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6w OCA], [https://pdbe.org/1i6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6w RCSB], [https://www.ebi.ac.uk/pdbsum/1i6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ESTA_BACSU ESTA_BACSU] Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.<ref>PMID:8396026</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/i6/1i6w_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=1i6w ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1I6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I6W OCA].
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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==Reference==
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<references/>
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The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme., van Pouderoyen G, Eggert T, Jaeger KE, Dijkstra BW, J Mol Biol. 2001 May 25;309(1):215-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11491291 11491291]
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Dijkstra BW]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Eggert T]]
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[[Category: Eggert, T.]]
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[[Category: Jaeger K-E]]
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[[Category: Jaeger, K.E.]]
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[[Category: Van Pouderoyen G]]
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[[Category: Pouderoyen, G.van.]]
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[[Category: CD]]
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[[Category: alpha/beta hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:06:42 2007''
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Current revision

THE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE: A MINIMAL ALPHA/BETA HYDROLASE ENZYME

PDB ID 1i6w

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