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| | ==The complex of pOPH_S172A of pNPB== | | ==The complex of pOPH_S172A of pNPB== |
| - | <StructureSection load='3wwc' size='340' side='right' caption='[[3wwc]], [[Resolution|resolution]] 1.49Å' scene=''> | + | <StructureSection load='3wwc' size='340' side='right'caption='[[3wwc]], [[Resolution|resolution]] 1.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wwc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._vm15c Pseudomonas sp. vm15c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WWC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wwc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._VM15C Pseudomonas sp. VM15C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WWC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BUA:BUTANOIC+ACID'>BUA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 1.49Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wwe|3wwe]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BUA:BUTANOIC+ACID'>BUA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pvaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237605 Pseudomonas sp. VM15C])</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=3wwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwc OCA], [https://pdbe.org/3wwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wwc RCSB], [https://www.ebi.ac.uk/pdbsum/3wwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwc 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/Beta-diketone_hydrolase Beta-diketone hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.7 3.7.1.7] </span></td></tr>
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| - | <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=3wwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwc OCA], [http://pdbe.org/3wwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wwc RCSB], [http://www.ebi.ac.uk/pdbsum/3wwc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OPH_PSESP OPH_PSESP] |
| | <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: Beta-diketone hydrolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas sp. vm15c]] | + | [[Category: Pseudomonas sp. VM15C]] |
| - | [[Category: Chen, J]] | + | [[Category: Chen J]] |
| - | [[Category: Du, G C]] | + | [[Category: Du GC]] |
| - | [[Category: Guo, R T]] | + | [[Category: Guo RT]] |
| - | [[Category: Huang, C H]] | + | [[Category: Huang CH]] |
| - | [[Category: Ko, T P]] | + | [[Category: Ko TP]] |
| - | [[Category: Li, J H]] | + | [[Category: Li JH]] |
| - | [[Category: Liu, L]] | + | [[Category: Liu L]] |
| - | [[Category: Yang, Y]] | + | [[Category: Yang Y]] |
| - | [[Category: Disulfide bridge]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: P-nitrophenyl ester]]
| + | |
| - | [[Category: Tryptophan]]
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| Structural highlights
Function
OPH_PSESP
Publication Abstract from PubMed
Oxidized polyvinyl alcohol hydrolase (OPH) catalyzes the cleavage of C-C bond in beta-diketone. It belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site. The lid is the most variable region when pOPH from Pseudomonas sp. VM15C and sOPH from Sphingopyxis sp. 113P3 are compared. The wild-type enzymes and the pOPH mutants W255A, W255Y and W255F were analyzed for lipase activity by using p-nitrophenyl (pNP) esters as the substrates. The wild-type enzymes showed increased Km and decreased kcat/Km with the acyl chain length, and the mutants showed reduced kcat/Km for pNP acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for pNP butyrate can be a result of product inhibition, as suggested by the complex crystal structures, in which butyric acid, DMSO or PEG occupied the same substrate-binding cleft. The mutant activity was retained with pNP caprylate and pNP laurate as the substrates, reflecting the amphipathic nature of the cleft. Moreover, the disulfide bond formation of Cys257/267 is important for the activity of pOPH, but it is not essential for sOPH, which has a shorter lid structure.
Roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase.,Yang Y, Ko TP, Liu L, Li J, Huang CH, Chen J, Guo RT, Du G Biochem Biophys Res Commun. 2014 Sep 26;452(3):509-14. doi:, 10.1016/j.bbrc.2014.08.106. Epub 2014 Aug 27. PMID:25173935[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang Y, Ko TP, Liu L, Li J, Huang CH, Chen J, Guo RT, Du G. Roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase. Biochem Biophys Res Commun. 2014 Sep 26;452(3):509-14. doi:, 10.1016/j.bbrc.2014.08.106. Epub 2014 Aug 27. PMID:25173935 doi:http://dx.doi.org/10.1016/j.bbrc.2014.08.106
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