1enp
From Proteopedia
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'''BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE''' | '''BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE''' | ||
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Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase., Rafferty JB, Simon JW, Baldock C, Artymiuk PJ, Baker PJ, Stuitje AR, Slabas AR, Rice DW, Structure. 1995 Sep 15;3(9):927-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535786 8535786] | Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase., Rafferty JB, Simon JW, Baldock C, Artymiuk PJ, Baker PJ, Stuitje AR, Slabas AR, Rice DW, Structure. 1995 Sep 15;3(9):927-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535786 8535786] | ||
[[Category: Brassica napus]] | [[Category: Brassica napus]] | ||
| - | [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Rafferty, J B.]] | [[Category: Rafferty, J B.]] | ||
[[Category: Rice, D W.]] | [[Category: Rice, D W.]] | ||
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Plant lipid biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:19:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:19, 2 May 2008
BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE
Overview
BACKGROUND: Enoyl acyl carrier protein reductase (ENR) catalyzes the NAD(P)H-dependent reduction of trans-delta 2-enoyl acyl carrier protein, an essential step in de novo fatty acid biosynthesis. Plants contain both NADH-dependent and separate NADPH-dependent ENR enzymes which form part of the dissociable type II fatty acid synthetase. Highly elevated levels of the NADH-dependent enzyme are found during lipid deposition in maturing seeds of oilseed rape (Brassica napus). RESULTS: The crystal structure of an ENR-NAD binary complex has been determined at 1.9 A resolution and consists of a homotetramer in which each subunit forms a single domain comprising a seven-stranded parallel beta sheet flanked by seven alpha helices. The subunit has a topology highly reminiscent of a dinucleotide-binding fold. The active site has been located by difference Fourier analysis of data from crystals equilibrated in NADH. CONCLUSIONS: The structure of ENR shows a striking similarity with the epimerases and short-chain alcohol dehydrogenases, in particular, 3 alpha,20 beta-hydroxysteroid dehydrogenase (HSD). The similarity with HSD extends to the conservation of a catalytically important lysine that stabilizes the transition state and to the use of a tyrosine as a base--with subtle modifications arising from differing requirements of the reduction chemistry.
About this Structure
1ENP is a Single protein structure of sequence from Brassica napus. Full crystallographic information is available from OCA.
Reference
Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase., Rafferty JB, Simon JW, Baldock C, Artymiuk PJ, Baker PJ, Stuitje AR, Slabas AR, Rice DW, Structure. 1995 Sep 15;3(9):927-38. PMID:8535786 Page seeded by OCA on Fri May 2 15:19:08 2008
