1dub
From Proteopedia
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|PDB= 1dub |SIZE=350|CAPTION= <scene name='initialview01'>1dub</scene>, resolution 2.5Å | |PDB= 1dub |SIZE=350|CAPTION= <scene name='initialview01'>1dub</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=CR1:Catalytic+Residue+1'>CR1</scene> and <scene name='pdbsite=CR2:Catalytic+Residue+2'>CR2</scene> | |SITE= <scene name='pdbsite=CR1:Catalytic+Residue+1'>CR1</scene> and <scene name='pdbsite=CR2:Catalytic+Residue+2'>CR2</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME A'>CAA</scene> | + | |LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dub OCA], [http://www.ebi.ac.uk/pdbsum/1dub PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dub RCSB]</span> | ||
}} | }} | ||
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[[Category: Engel, C K.]] | [[Category: Engel, C K.]] | ||
[[Category: Wierenga, R K.]] | [[Category: Wierenga, R K.]] | ||
| - | [[Category: CAA]] | ||
[[Category: beta-oxidation]] | [[Category: beta-oxidation]] | ||
[[Category: coa]] | [[Category: coa]] | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:47 2008'' |
Revision as of 16:48, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Enoyl-CoA hydratase, with EC number 4.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5
Overview
The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme catalyses the reversible addition of water to alpha,beta-unsaturated enoyl-CoA thioesters, with nearly diffusion-controlled reaction rates for the best substrates. Enoyl-CoA hydratase is a hexamer of six identical subunits of 161 kDa molecular mass for the complex. The hexamer is a dimer of trimers. The monomer is folded into a right-handed spiral of four turns, followed by two small domains which are involved in trimerization. Each turn of the spiral consists of two beta-strands and an alpha-helix. The mechanism for the hydratase/dehydratase reaction follows a syn-stereochemistry, a preference that is opposite to the nonenzymatic reaction. The active-site architecture agrees with this stereochemistry. It confirms the importance of Glu164 as the catalytic acid for providing the alpha-proton during the hydratase reaction. It also shows the importance of Glu144 as the catalytic base for the activation of a water molecule in the hydratase reaction. The comparison of an unliganded and a liganded active site within the same crystal form shows a water molecule in the unliganded subunit. This water molecule is bound between the two catalytic glutamates and could serve as the activated water during catalysis.
About this Structure
1DUB is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket., Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK, EMBO J. 1996 Oct 1;15(19):5135-45. PMID:8895557
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