1enp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1enp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1enp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1enp| PDB=1enp | SCENE= }}
{{STRUCTURE_1enp| PDB=1enp | SCENE= }}
-
'''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===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8535786}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8535786 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8535786}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Plant lipid biosynthesis]]
[[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 Tue Jul 1 01:08:59 2008''

Revision as of 22:09, 30 June 2008

Image:1enp.png

Template:STRUCTURE 1enp

BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE

Template:ABSTRACT PUBMED 8535786

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 Tue Jul 1 01:08:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1enp"
Personal tools