From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1dub.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1dub.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1dub| PDB=1dub | SCENE= }} | | {{STRUCTURE_1dub| PDB=1dub | SCENE= }} |
| | | | |
| - | '''2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8895557}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8895557 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8895557}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Fatty acid metabolism]] | | [[Category: Fatty acid metabolism]] |
| | [[Category: Lyase]] | | [[Category: Lyase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:17:01 2008'' | + | |
| | + | ''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
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
