1dub
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1dub.jpg|left|200px]] | + | [[Image:1dub.jpg|left|200px]] |
| - | + | ||
| - | '''2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5''' | + | {{Structure |
| + | |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> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1DUB is a [ | + | 1DUB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUB OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8895557 8895557] |
[[Category: Enoyl-CoA hydratase]] | [[Category: Enoyl-CoA hydratase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| Line 24: | Line 33: | ||
[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:34 2008'' |
Revision as of 08:44, 20 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Enoyl-CoA hydratase, with EC number 4.2.1.17 | ||||||
| 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
Page seeded by OCA on Thu Mar 20 10:44:34 2008
