1e5q
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(New page: 200px<br /> <applet load="1e5q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5q, resolution 2.10Å" /> '''TERNARY COMPLEX OF ...)
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Revision as of 14:50, 29 October 2007
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TERNARY COMPLEX OF SACCHAROPINE REDUCTASE FROM MAGNAPORTHE GRISEA, NADPH AND SACCHAROPINE
Overview
BACKGROUND: The biosynthesis of the essential amino acid lysine in higher, fungi and cyanobacteria occurs via the alpha-aminoadipate pathway, which, is completely different from the lysine biosynthetic pathway found in, plants and bacteria. The penultimate reaction in the alpha-aminoadipate, pathway is catalysed by NADPH-dependent saccharopine reductase. We set out, to determine the structure of this enzyme as a first step in exploring the, structural biology of fungal lysine biosynthesis. RESULTS: We have, determined the three-dimensional structure of saccharopine reductase from, the plant pathogen Magnaporthe grisea in its apo form to 2.0 A resolution, and as a ternary complex with NADPH and saccharopine to 2.1 A resolution., Saccharopine reductase is a homodimer, and each subunit ... [(full description)]
About this Structure
1E5Q is a [Single protein] structure of sequence from [Magnaporthe grisea] with NDP and SHR as [ligands]. Active as [[1]], with EC number [1.5.1.10]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis., Johansson E, Steffens JJ, Lindqvist Y, Schneider G, Structure. 2000 Oct 15;8(10):1037-47. PMID:11080625
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