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| | <StructureSection load='1iq6' size='340' side='right'caption='[[1iq6]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1iq6' size='340' side='right'caption='[[1iq6]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iq6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aeromonas_caviae"_eddy_1962 "aeromonas caviae" eddy 1962]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IQ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iq6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_caviae Aeromonas caviae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IQ6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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]] 1.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></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=1iq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iq6 OCA], [https://pdbe.org/1iq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1iq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iq6 ProSAT]</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=1iq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iq6 OCA], [https://pdbe.org/1iq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1iq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iq6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHAJ_AERCA PHAJ_AERCA]] Catalyzes the hydration of trans-2-enoyl-CoA with a chain-length of 4-6 carbon atoms, forming the corresponding (3R)-3-hydroxyacyl-CoA.<ref>PMID:9244271</ref> <ref>PMID:9457873</ref>
| + | [https://www.uniprot.org/uniprot/PHAJ_AERCA PHAJ_AERCA] Catalyzes the hydration of trans-2-enoyl-CoA with a chain-length of 4-6 carbon atoms, forming the corresponding (3R)-3-hydroxyacyl-CoA.<ref>PMID:9244271</ref> <ref>PMID:9457873</ref> |
| | == 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: Aeromonas caviae eddy 1962]] | |
| - | [[Category: Enoyl-CoA hydratase]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Doi, Y]] | |
| - | [[Category: Fukui, T]] | |
| - | [[Category: Hisano, T]] | |
| - | [[Category: Iwata, T]] | |
| - | [[Category: Tsuge, T]] | |
| | [[Category: Aeromonas caviae]] | | [[Category: Aeromonas caviae]] |
| - | [[Category: Enoyl-coa hydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Hydratase]] | + | [[Category: Doi Y]] |
| - | [[Category: Lyase]] | + | [[Category: Fukui T]] |
| - | [[Category: Polyhydroxyalkanoate]] | + | [[Category: Hisano T]] |
| - | [[Category: The hydratase 2 motif]] | + | [[Category: Iwata T]] |
| | + | [[Category: Tsuge T]] |
| Structural highlights
Function
PHAJ_AERCA Catalyzes the hydration of trans-2-enoyl-CoA with a chain-length of 4-6 carbon atoms, forming the corresponding (3R)-3-hydroxyacyl-CoA.[1] [2]
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
The (R)-specific enoyl coenzyme A hydratase ((R)-hydratase) from Aeromonas caviae catalyzes the addition of a water molecule to trans-2-enoyl coenzyme A (CoA), with a chain-length of 4-6 carbons, to produce the corresponding (R)-3-hydroxyacyl-CoA. It forms a dimer of identical subunits with a molecular weight of about 14,000 and is involved in polyhydroxyalkanoate (PHA) biosynthesis. The crystal structure of the enzyme has been determined at 1.5-A resolution. The structure of the monomer consists of a five-stranded antiparallel beta-sheet and a central alpha-helix, folded into a so-called "hot dog" fold, with an overhanging segment. This overhang contains the conserved residues including the hydratase 2 motif residues. In dimeric form, two beta-sheets are associated to form an extended 10-stranded beta-sheet, and the overhangs obscure the putative active sites at the subunit interface. The active site is located deep within the substrate-binding tunnel, where Asp(31) and His(36) form a catalytic dyad. These residues are catalytically important as confirmed by site-directed mutagenesis and are possibly responsible for the activation of a water molecule and the protonation of a substrate molecule, respectively. Residues such as Leu(65) and Val(130) are situated at the bottom of the substrate-binding tunnel, defining the preference of the enzyme for the chain length of the substrate. These results provide target residues for protein engineering, which will enhance the significance of this enzyme in the production of novel PHA polymers. In addition, this study provides the first structural information of the (R)-hydratase family and may facilitate further functional studies for members of the family.
Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis.,Hisano T, Tsuge T, Fukui T, Iwata T, Miki K, Doi Y J Biol Chem. 2003 Jan 3;278(1):617-24. Epub 2002 Oct 29. PMID:12409309[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fukui T, Doi Y. Cloning and analysis of the poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis genes of Aeromonas caviae. J Bacteriol. 1997 Aug;179(15):4821-30. PMID:9244271
- ↑ Fukui T, Shiomi N, Doi Y. Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae. J Bacteriol. 1998 Feb;180(3):667-73. PMID:9457873
- ↑ Hisano T, Tsuge T, Fukui T, Iwata T, Miki K, Doi Y. Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis. J Biol Chem. 2003 Jan 3;278(1):617-24. Epub 2002 Oct 29. PMID:12409309 doi:10.1074/jbc.M205484200
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