1gyr
From Proteopedia
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| - | [[Image:1gyr.gif|left|200px]] | + | [[Image:1gyr.gif|left|200px]] |
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| - | '''MUTANT FORM OF ENOYL THIOESTER REDUCTASE FROM CANDIDA TROPICALIS''' | + | {{Structure |
| + | |PDB= 1gyr |SIZE=350|CAPTION= <scene name='initialview01'>1gyr</scene>, resolution 2.6Å | ||
| + | |SITE= <scene name='pdbsite=GA1:So4+Binding+Site+For+Chain+A'>GA1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''MUTANT FORM OF ENOYL THIOESTER REDUCTASE FROM CANDIDA TROPICALIS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GYR is a [ | + | 1GYR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYR OCA]. |
==Reference== | ==Reference== | ||
| - | Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance., Airenne TT, Torkko JM, Van den plas S, Sormunen RT, Kastaniotis AJ, Wierenga RK, Hiltunen JK, J Mol Biol. 2003 Mar 14;327(1):47-59. PMID:[http:// | + | Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance., Airenne TT, Torkko JM, Van den plas S, Sormunen RT, Kastaniotis AJ, Wierenga RK, Hiltunen JK, J Mol Biol. 2003 Mar 14;327(1):47-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12614607 12614607] |
[[Category: Candida tropicalis]] | [[Category: Candida tropicalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 11:29:47 2008'' |
Revision as of 09:29, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MUTANT FORM OF ENOYL THIOESTER REDUCTASE FROM CANDIDA TROPICALIS
Overview
Candida tropicalis enoyl thioester reductase Etr1p and the Saccharomyces cerevisiae homologue Mrf1p catalyse the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (FAS). Unlike prokaryotic enoyl thioester reductases (ETRs), which belong to the short-chain dehydrogenases/reductases (SDR), Etr1p and Mrf1p represent structurally distinguishable ETRs that belong to the medium-chain dehydrogenases/reductases (MDR) superfamily, indicating independent origin of two separate classes of ETRs. The crystal structures of Etr1p, the Etr1p-NADPH complex and the Etr1Y79Np mutant were refined to 1.70A, 2.25A and 2.60A resolution, respectively. The native fold of Etr1p was maintained in Etr1Y79Np, but the mutant had only 0.1% of Etr1p catalytic activity remaining and failed to rescue the respiratory deficient phenotype of the mrf1Delta strain. Mutagenesis of Tyr73 in Mrf1p, corresponding to Tyr79 in Etr1p, produced similar results. Our data indicate that the mitochondrial reductase activity is indispensable for respiratory function in yeast, emphasizing the significance of Mrf1p (Etr1p) and mitochondrial FAS for the integrity of the respiratory competent organelle.
About this Structure
1GYR is a Single protein structure of sequence from Candida tropicalis. Full crystallographic information is available from OCA.
Reference
Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance., Airenne TT, Torkko JM, Van den plas S, Sormunen RT, Kastaniotis AJ, Wierenga RK, Hiltunen JK, J Mol Biol. 2003 Mar 14;327(1):47-59. PMID:12614607
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