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1dub

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{{STRUCTURE_1dub| PDB=1dub | SCENE= }}
{{STRUCTURE_1dub| PDB=1dub | SCENE= }}
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'''2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5'''
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===2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8895557 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8895557}}
==About this Structure==
==About this Structure==
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[[Category: Fatty acid metabolism]]
[[Category: Fatty acid metabolism]]
[[Category: Lyase]]
[[Category: Lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:37:39 2008''

Revision as of 20:37, 30 June 2008

Image:1dub.png

Template:STRUCTURE 1dub

2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5

Template:ABSTRACT PUBMED 8895557

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 Mon Jun 30 23:37:39 2008

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