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| | ==Crystal structure of Bacillus subtilis lipase at 1.3A resolution== | | ==Crystal structure of Bacillus subtilis lipase at 1.3A resolution== |
| - | <StructureSection load='1isp' size='340' side='right' caption='[[1isp]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='1isp' size='340' side='right'caption='[[1isp]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1isp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ISP FirstGlance]. <br> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr> | + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <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> |
| - | <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=1isp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1isp OCA], [http://pdbe.org/1isp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1isp RCSB], [http://www.ebi.ac.uk/pdbsum/1isp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1isp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1isp" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1isp" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Lipase 3D Structures|Lipase 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Triacylglycerol lipase]] | + | [[Category: Large Structures]] |
| - | [[Category: Kawasaki, K]] | + | [[Category: Kawasaki K]] |
| - | [[Category: Kondo, H]] | + | [[Category: Kondo H]] |
| - | [[Category: Ohgiya, S]] | + | [[Category: Ohgiya S]] |
| - | [[Category: Suzuki, M]] | + | [[Category: Suzuki M]] |
| - | [[Category: Tsuda, S]] | + | [[Category: Tsuda S]] |
| - | [[Category: Alpha/beta hydrolase fold]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
ESTA_BACSU Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lesuisse E, Schanck K, Colson C. Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme. Eur J Biochem. 1993 Aug 15;216(1):155-60. PMID:8396026
- ↑ Kawasaki K, Kondo H, Suzuki M, Ohgiya S, Tsuda S. Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution. Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1168-74. Epub 2002, Jun 20. PMID:12077437
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