1isp

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[[Image:1isp.jpg|left|200px]]
 
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==Crystal structure of Bacillus subtilis lipase at 1.3A resolution==
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The line below this paragraph, containing "STRUCTURE_1isp", creates the "Structure Box" on the page.
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<StructureSection load='1isp' size='340' side='right'caption='[[1isp]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1isp]] is a 1 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=1ISP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ISP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.3&#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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{{STRUCTURE_1isp| PDB=1isp | SCENE= }}
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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=1isp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1isp OCA], [https://pdbe.org/1isp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1isp RCSB], [https://www.ebi.ac.uk/pdbsum/1isp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1isp 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/is/1isp_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=1isp ConSurf].
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<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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Bacillus subtilis extracellular lipase (BsL) has an exceptionally low molecular weight (19.4 kDa) for a member of the lipase family. A crystallographic study was performed on BsL in order to design and produce mutant BsL that will be more suitable for industrial uses based on analysis of the three-dimensional structure. Recently, the crystal structure of BsL has been determined at 1.5 A resolution [van Pouderoyen et al. (2001). J. Mol. Biol. 309, 215-226]. In the present study, a new crystal form of BsL which provides diffraction data to higher resolution was obtained and its structure was determined at 1.3 A using the MAD method. It was found that the active-site residue Ser77 has alternate side-chain conformations. The O(gamma) atom of the first conformer forms a hydrogen bond to the N(epsilon) atom of His155, a member of the catalytic triad. In contrast, the second conformer is constructed with a hydrogen bond to the side-chain atom of the adjacent His76. These two conformers presumably correspond to the active and inactive states, respectively. Similar alternate conformations in the catalytic serine residue have been observed in Fusarium solani cutinase determined at 1.0 A resolution and Penicillium purpurogenum acetylxylan esterase at 0.9 A resolution. In addition, a glycerol molecule, which was used as a cryoprotectant, is found to be located in the active site. On the basis of these results, a model for substrate binding in the reaction-intermediate state of BsL is proposed.
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'''Crystal structure of Bacillus subtilis lipase at 1.3A resolution'''
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Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.,Kawasaki K, Kondo H, Suzuki M, Ohgiya S, Tsuda S Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1168-74. Epub 2002, Jun 20. PMID:12077437<ref>PMID:12077437</ref>
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==Overview==
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Bacillus subtilis extracellular lipase (BsL) has an exceptionally low molecular weight (19.4 kDa) for a member of the lipase family. A crystallographic study was performed on BsL in order to design and produce mutant BsL that will be more suitable for industrial uses based on analysis of the three-dimensional structure. Recently, the crystal structure of BsL has been determined at 1.5 A resolution [van Pouderoyen et al. (2001). J. Mol. Biol. 309, 215-226]. In the present study, a new crystal form of BsL which provides diffraction data to higher resolution was obtained and its structure was determined at 1.3 A using the MAD method. It was found that the active-site residue Ser77 has alternate side-chain conformations. The O(gamma) atom of the first conformer forms a hydrogen bond to the N(epsilon) atom of His155, a member of the catalytic triad. In contrast, the second conformer is constructed with a hydrogen bond to the side-chain atom of the adjacent His76. These two conformers presumably correspond to the active and inactive states, respectively. Similar alternate conformations in the catalytic serine residue have been observed in Fusarium solani cutinase determined at 1.0 A resolution and Penicillium purpurogenum acetylxylan esterase at 0.9 A resolution. In addition, a glycerol molecule, which was used as a cryoprotectant, is found to be located in the active site. On the basis of these results, a model for substrate binding in the reaction-intermediate state of BsL is proposed.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1ISP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ISP OCA].
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</div>
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<div class="pdbe-citations 1isp" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution., Kawasaki K, Kondo H, Suzuki M, Ohgiya S, Tsuda S, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1168-74. Epub 2002, Jun 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12077437 12077437]
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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<references/>
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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: Kawasaki K]]
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[[Category: Kawasaki, K.]]
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[[Category: Kondo H]]
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[[Category: Kondo, H.]]
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[[Category: Ohgiya S]]
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[[Category: Ohgiya, S.]]
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[[Category: Suzuki M]]
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[[Category: Suzuki, M.]]
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[[Category: Tsuda S]]
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[[Category: Tsuda, S.]]
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[[Category: Alpha/beta hydrolase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:22:10 2008''
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Current revision

Crystal structure of Bacillus subtilis lipase at 1.3A resolution

PDB ID 1isp

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