1ps9
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ps9.jpg|left|200px]] | [[Image:1ps9.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ps9", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1ps9| PDB=1ps9 | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''The Crystal Structure and Reaction Mechanism of E. coli 2,4-Dienoyl CoA Reductase''' | '''The Crystal Structure and Reaction Mechanism of E. coli 2,4-Dienoyl CoA Reductase''' | ||
| Line 23: | Line 20: | ||
==Reference== | ==Reference== | ||
The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase., Hubbard PA, Liang X, Schulz H, Kim JJ, J Biol Chem. 2003 Sep 26;278(39):37553-60. Epub 2003 Jul 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12840019 12840019] | The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase., Hubbard PA, Liang X, Schulz H, Kim JJ, J Biol Chem. 2003 Sep 26;278(39):37553-60. Epub 2003 Jul 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12840019 12840019] | ||
| - | [[Category: 2,4-dienoyl-CoA reductase (NADPH)]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 30: | Line 26: | ||
[[Category: Liang, X.]] | [[Category: Liang, X.]] | ||
[[Category: Schulz, H.]] | [[Category: Schulz, H.]] | ||
| - | [[Category: | + | [[Category: Electron transfer]] |
| - | [[Category: | + | [[Category: Flavin]] |
| - | [[Category: | + | [[Category: Flavodoxin]] |
| - | [[Category: | + | [[Category: Hydride transfer]] |
| - | [[Category: | + | [[Category: Iron-sulfur]] |
| - | [[Category: | + | [[Category: Tim barrel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:25:49 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:25, 3 May 2008
The Crystal Structure and Reaction Mechanism of E. coli 2,4-Dienoyl CoA Reductase
Overview
Escherichia coli 2,4-dienoyl-CoA reductase is an iron-sulfur flavoenzyme required for the metabolism of unsaturated fatty acids with double bonds at even carbon positions. The enzyme contains FMN, FAD, and a 4Fe-4S cluster and exhibits sequence homology to another iron-sulfur flavoprotein, trimethylamine dehydrogenase. It also requires NADPH as an electron source, resulting in reduction of the C4-C5 double bond of the acyl chain of the CoA thioester substrate. The structure presented here of a ternary complex of E. coli 2,4-dienoyl-CoA reductase with NADP+ and a fatty acyl-CoA substrate reveals a possible mechanism for substrate reduction and provides details of a plausible electron transfer mechanism involving both flavins and the iron-sulfur cluster. The reaction is initiated by hydride transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. In the final stages of the reaction, the fully reduced FMN provides a hydride ion to the C5 atom of substrate, and Tyr-166 and His-252 are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and complete the reaction. Inspection of the substrate binding pocket explains the relative promiscuity of the enzyme, catalyzing reduction of both 2-trans,4-cis- and 2-trans,4-trans-dienoyl-CoA thioesters.
About this Structure
1PS9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase., Hubbard PA, Liang X, Schulz H, Kim JJ, J Biol Chem. 2003 Sep 26;278(39):37553-60. Epub 2003 Jul 2. PMID:12840019 Page seeded by OCA on Sat May 3 05:25:49 2008
