1edo
From Proteopedia
(New page: 200px<br /><applet load="1edo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1edo, resolution 2.3Å" /> '''THE X-RAY STRUCTURE O...) |
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| - | [[Image:1edo.gif|left|200px]]<br /><applet load="1edo" size=" | + | [[Image:1edo.gif|left|200px]]<br /><applet load="1edo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1edo, resolution 2.3Å" /> | caption="1edo, resolution 2.3Å" /> | ||
'''THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+'''<br /> | '''THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: beta-Keto acyl carrier protein reductase (BKR) catalyzes the | + | BACKGROUND: beta-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. RESULTS: The first crystal structure of BKR has been determined at 2.3 A resolution in a binary complex with an NADP(+) cofactor. The structure reveals a homotetramer in which each subunit has a classical dinucleotide-binding fold. A triad of Ser154, Tyr167 and Lys171 residues is found at the active site, characteristic of the SDR family. Overall BKR has a very similar structure to ENR with good superimposition of catalytically important groups. Modelling of the substrate into the active site of BKR indicates the need for conformational changes in the enzyme. CONCLUSIONS: A catalytic mechanism can be proposed involving the conserved triad. Helix alpha6 must shift its position to permit substrate binding to BKR and might act as a flexible lid on the active site. The similarities in fold, mechanism and substrate binding between BKR, which catalyzes a carbon-oxygen double-bond reduction, and ENR, the carbon-carbon double-bond oxidoreductase in FAS, suggest a close evolutionary link during the development of the fatty acid biosynthetic pathway. |
==About this Structure== | ==About this Structure== | ||
| - | 1EDO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus] with NAP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EDO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus] with <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fisher, M.]] | [[Category: Fisher, M.]] | ||
| - | [[Category: Kroon, J | + | [[Category: Kroon, J T.]] |
[[Category: Martindale, W.]] | [[Category: Martindale, W.]] | ||
| - | [[Category: Rafferty, J | + | [[Category: Rafferty, J B.]] |
| - | [[Category: Slabas, A | + | [[Category: Slabas, A R.]] |
| - | [[Category: Stuitje, A | + | [[Category: Stuitje, A R.]] |
[[Category: NAP]] | [[Category: NAP]] | ||
[[Category: nucleotide fold]] | [[Category: nucleotide fold]] | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:39 2008'' |
Revision as of 10:26, 21 February 2008
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THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+
Overview
BACKGROUND: beta-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. RESULTS: The first crystal structure of BKR has been determined at 2.3 A resolution in a binary complex with an NADP(+) cofactor. The structure reveals a homotetramer in which each subunit has a classical dinucleotide-binding fold. A triad of Ser154, Tyr167 and Lys171 residues is found at the active site, characteristic of the SDR family. Overall BKR has a very similar structure to ENR with good superimposition of catalytically important groups. Modelling of the substrate into the active site of BKR indicates the need for conformational changes in the enzyme. CONCLUSIONS: A catalytic mechanism can be proposed involving the conserved triad. Helix alpha6 must shift its position to permit substrate binding to BKR and might act as a flexible lid on the active site. The similarities in fold, mechanism and substrate binding between BKR, which catalyzes a carbon-oxygen double-bond reduction, and ENR, the carbon-carbon double-bond oxidoreductase in FAS, suggest a close evolutionary link during the development of the fatty acid biosynthetic pathway.
About this Structure
1EDO is a Single protein structure of sequence from Brassica napus with as ligand. Full crystallographic information is available from OCA.
Reference
The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis., Fisher M, Kroon JT, Martindale W, Stuitje AR, Slabas AR, Rafferty JB, Structure. 2000 Apr 15;8(4):339-47. PMID:10801480
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