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| | ==Crystal structure of a thermostable lipase from Marine Streptomyces== | | ==Crystal structure of a thermostable lipase from Marine Streptomyces== |
| - | <StructureSection load='5h6b' size='340' side='right' caption='[[5h6b]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5h6b' size='340' side='right'caption='[[5h6b]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h6b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp._w007 Streptomyces sp. w007]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H6B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._W007 Streptomyces sp. W007]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H6B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h6g|5h6g]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPW_1544 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1055352 Streptomyces sp. W007])</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=5h6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h6b OCA], [https://pdbe.org/5h6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h6b RCSB], [https://www.ebi.ac.uk/pdbsum/5h6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h6b ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5h6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h6b OCA], [http://pdbe.org/5h6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h6b RCSB], [http://www.ebi.ac.uk/pdbsum/5h6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h6b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/H0B8D4_9ACTN H0B8D4_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces sp. w007]] | + | [[Category: Large Structures]] |
| - | [[Category: Triacylglycerol lipase]] | + | [[Category: Streptomyces sp. W007]] |
| - | [[Category: Hou, S]] | + | [[Category: Hou S]] |
| - | [[Category: Liu, J]] | + | [[Category: Liu J]] |
| - | [[Category: Zhao, Z]] | + | [[Category: Zhao Z]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Lipase]]
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| - | [[Category: Marine]]
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| - | [[Category: Thermostability]]
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| Structural highlights
Function
H0B8D4_9ACTN
Publication Abstract from PubMed
MAS1 from marine Streptomyces sp. strain W007 belongs to the bacterial lipase I.7 subfamily, and is characterized as a thermostable and non-regiospecific lipase. To shed light on the catalytic mechanism of MAS1, we determined its crystal structure with closed conformation in two crystal forms at 2.3-A resolution. MAS1 adopts the canonical alpha/beta hydrolase core fold with its catalytic triad being formed by S109, D200 and H232. Structural analysis and biochemical assays revealed that disulfide bonds and salt bridges play a vital role in the thermostability of MAS1. Additionally, we discovered that the substitution of H108 with a tryptophan converts MAS1 from a non-regiospecific to an sn-1, 3 specific lipase, suggesting the functional importance of the second position from the conserved pentapeptide motif in defining the regiospecificity of MAS1. Our present study provides insights into the molecular basis for the thermostability and regiospecificity of MAS1, and may aid in the rational design of thermostable or regiospecific lipases for potential industrial applications. This article is protected by copyright. All rights reserved.
Crystal structure of a lipase from Streptomyces sp. strain W007:implications for thermostability and regiospecificity.,Zhao Z, Hou S, Lan D, Wang X, Liu J, Khan FI, Wang Y FEBS J. 2017 Aug 31. doi: 10.1111/febs.14211. PMID:28857479[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao Z, Hou S, Lan D, Wang X, Liu J, Khan FI, Wang Y. Crystal structure of a lipase from Streptomyces sp. strain W007:implications for thermostability and regiospecificity. FEBS J. 2017 Aug 31. doi: 10.1111/febs.14211. PMID:28857479 doi:http://dx.doi.org/10.1111/febs.14211
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