1gyr

From Proteopedia

(Difference between revisions)

Revision as of 06:35, 3 January 2018

Mutant form of enoyl thioester reductase from Candida tropicalis

Structural highlights

1gyr is a 3 chain structure with sequence from Atcc 4563. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1gu7, 1guf
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ETR1_CANTR] Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Torkko JM, Koivuranta KT, Miinalainen IJ, Yagi AI, Schmitz W, Kastaniotis AJ, Airenne TT, Gurvitz A, Hiltunen KJ. Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence. Mol Cell Biol. 2001 Sep;21(18):6243-53. PMID:11509667
↑ Airenne TT, Torkko JM, Van den plas S, Sormunen RT, Kastaniotis AJ, Wierenga RK, Hiltunen JK. Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance. J Mol Biol. 2003 Mar 14;327(1):47-59. PMID:12614607

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gyr"

@@ Line 1: / Line 1: @@
-==MUTANT FORM OF ENOYL THIOESTER REDUCTASE FROM CANDIDA TROPICALIS==
+==Mutant form of enoyl thioester reductase from Candida tropicalis==
 <StructureSection load='1gyr' size='340' side='right' caption='[[1gyr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gu7|1gu7]], [[1guf|1guf]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyr OCA], [http://pdbe.org/1gyr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gyr RCSB], [http://www.ebi.ac.uk/pdbsum/1gyr PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyr OCA], [http://pdbe.org/1gyr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gyr RCSB], [http://www.ebi.ac.uk/pdbsum/1gyr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyr ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gyr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gyr_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1gyr

From Proteopedia

Revision as of 06:35, 3 January 2018

Mutant form of enoyl thioester reductase from Candida tropicalis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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