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| | ==meta-Cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) S103A mutant complexed with isobutyrates== | | ==meta-Cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) S103A mutant complexed with isobutyrates== |
| - | <StructureSection load='1iup' size='340' side='right' caption='[[1iup]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='1iup' size='340' side='right'caption='[[1iup]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iup]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IUP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALQ:2-METHYL-PROPIONIC+ACID'>ALQ</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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iun|1iun]], [[1iuo|1iuo]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALQ:2-METHYL-PROPIONIC+ACID'>ALQ</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cumD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 "Bacillus fluorescens liquefaciens" Flugge 1886])</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=1iup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iup OCA], [https://pdbe.org/1iup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iup RCSB], [https://www.ebi.ac.uk/pdbsum/1iup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iup 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/2-hydroxymuconate-6-semialdehyde_hydrolase 2-hydroxymuconate-6-semialdehyde hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.9 3.7.1.9] </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=1iup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iup OCA], [http://pdbe.org/1iup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iup RCSB], [http://www.ebi.ac.uk/pdbsum/1iup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iup ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P96965_PSEFL P96965_PSEFL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | + | [[Category: Large Structures]] |
| - | [[Category: 2-hydroxymuconate-6-semialdehyde hydrolase]] | + | [[Category: Pseudomonas fluorescens]] |
| - | [[Category: Fushinobu, S]] | + | [[Category: Fushinobu S]] |
| - | [[Category: Hidaka, M]] | + | [[Category: Hidaka M]] |
| - | [[Category: Jun, S Y]] | + | [[Category: Jun S-Y]] |
| - | [[Category: Nojiri, H]] | + | [[Category: Nojiri H]] |
| - | [[Category: Omori, T]] | + | [[Category: Omori T]] |
| - | [[Category: Saku, T]] | + | [[Category: Saku T]] |
| - | [[Category: Shoun, H]] | + | [[Category: Shoun H]] |
| - | [[Category: Wakagi, T]] | + | [[Category: Wakagi T]] |
| - | [[Category: Yamane, H]] | + | [[Category: Yamane H]] |
| - | [[Category: Alpha/beta-hydrolase]]
| + | |
| - | [[Category: Aromatic compound]]
| + | |
| - | [[Category: Beta-ketolase]]
| + | |
| - | [[Category: Cumene]]
| + | |
| - | [[Category: Cumene degradation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Isopropylbenzene]]
| + | |
| - | [[Category: Meta-cleavage compound hydrolase]]
| + | |
| - | [[Category: Pcb]]
| + | |
| - | [[Category: Polychlorinated biphenyl degradation]]
| + | |
| - | [[Category: Pseudomonas fluorescens ip01]]
| + | |
| - | [[Category: Substrate specificity]]
| + | |
| Structural highlights
Function
P96965_PSEFL
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
2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase (CumD) from Pseudomonas fluorescens IP01 hydrolyzes a meta-cleavage product generated in the cumene (isopropylbenzene) degradation pathway. The crystal structures of the inactive S103A mutant of the CumD enzyme complexed with isobutyrate and acetate ions were determined at 1.6 and 2.0 A resolution, respectively. The isobutyrate and acetate ions were located at the same position in the active site, and occupied the site for a part of the hydrolysis product with CumD, which has the key determinant group for the substrate specificity of related hydrolases. One of the oxygen atoms of the carboxyl group of the isobutyrate ion was hydrogen bonded with a water molecule and His252. Another oxygen atom of the carboxyl group was situated in an oxyanion hole formed by the two main-chain N atoms. The isopropyl group of the isobutyric acid was recognized by the side-chains of the hydrophobic residues. The substrate-binding pocket of CumD was long, and the inhibition constants of various organic acids corresponded well to it. In comparison with the structure of BphD from Rhodococcus sp. RHA1, the structural basis for the substrate specificity of related hydrolases, is revealed.
Crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with cleavage products.,Fushinobu S, Saku T, Hidaka M, Jun SY, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T Protein Sci. 2002 Sep;11(9):2184-95. PMID:12192074[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fushinobu S, Saku T, Hidaka M, Jun SY, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T. Crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with cleavage products. Protein Sci. 2002 Sep;11(9):2184-95. PMID:12192074
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