2p4h

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(New page: 200px<br /><applet load="2p4h" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p4h, resolution 1.40&Aring;" /> '''Crystal Structure of...)
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==Overview==
==Overview==
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Isoflavonoids are commonly found in leguminous plants, where they play, important roles in plant defense and have significant health benefits for, animals and humans. Vestitone reductase catalyzes a stereospecific, NADPH-dependent reduction of (3R)-vestitone in the biosynthesis of the, antimicrobial isoflavonoid phytoalexin medicarpin. The crystal structure, of alfalfa (Medicago sativa L.) vestitone reductase has been determined at, 1.4 A resolution. The structure contains a classic Rossmann fold domain in, the N terminus and a small C-terminal domain. Sequence and structural, analysis showed that vestitone reductase is a member of the short-chain, dehydrogenase/reductase (SDR) superfamily despite the low levels of, sequence identity, and the prominent structural differences from other SDR, enzymes with known structures. The putative binding sites for the, co-factor NADPH and the substrate (3R)-vestitone were defined and located, in a large cleft formed between the N and C-terminal domains of enzyme., Potential key residues for enzyme activity were also identified, including, the catalytic triad Ser129-Tyr164-Lys168. A molecular docking study showed, that (3R)-vestitone, but not the (3S) isomer, forms favored interactions, with the co-factor and catalytic triad, thus providing an explanation for, the enzyme's strict substrate stereo-specificity.
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Isoflavonoids are commonly found in leguminous plants, where they play important roles in plant defense and have significant health benefits for animals and humans. Vestitone reductase catalyzes a stereospecific NADPH-dependent reduction of (3R)-vestitone in the biosynthesis of the antimicrobial isoflavonoid phytoalexin medicarpin. The crystal structure of alfalfa (Medicago sativa L.) vestitone reductase has been determined at 1.4 A resolution. The structure contains a classic Rossmann fold domain in the N terminus and a small C-terminal domain. Sequence and structural analysis showed that vestitone reductase is a member of the short-chain dehydrogenase/reductase (SDR) superfamily despite the low levels of sequence identity, and the prominent structural differences from other SDR enzymes with known structures. The putative binding sites for the co-factor NADPH and the substrate (3R)-vestitone were defined and located in a large cleft formed between the N and C-terminal domains of enzyme. Potential key residues for enzyme activity were also identified, including the catalytic triad Ser129-Tyr164-Lys168. A molecular docking study showed that (3R)-vestitone, but not the (3S) isomer, forms favored interactions with the co-factor and catalytic triad, thus providing an explanation for the enzyme's strict substrate stereo-specificity.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.)., Shao H, Dixon RA, Wang X, J Mol Biol. 2007 May 25;369(1):265-76. Epub 2007 Mar 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17433362 17433362]
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Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.)., Shao H, Dixon RA, Wang X, J Mol Biol. 2007 May 25;369(1):265-76. Epub 2007 Mar 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17433362 17433362]
[[Category: Medicago sativa]]
[[Category: Medicago sativa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dixon, R.A.]]
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[[Category: Dixon, R A.]]
[[Category: Shao, H.]]
[[Category: Shao, H.]]
[[Category: Wang, X.]]
[[Category: Wang, X.]]
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[[Category: nadph-dependent reductase]]
[[Category: nadph-dependent reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:17:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:41 2008''

Revision as of 16:25, 21 February 2008


2p4h, resolution 1.40Å

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Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.)

Overview

Isoflavonoids are commonly found in leguminous plants, where they play important roles in plant defense and have significant health benefits for animals and humans. Vestitone reductase catalyzes a stereospecific NADPH-dependent reduction of (3R)-vestitone in the biosynthesis of the antimicrobial isoflavonoid phytoalexin medicarpin. The crystal structure of alfalfa (Medicago sativa L.) vestitone reductase has been determined at 1.4 A resolution. The structure contains a classic Rossmann fold domain in the N terminus and a small C-terminal domain. Sequence and structural analysis showed that vestitone reductase is a member of the short-chain dehydrogenase/reductase (SDR) superfamily despite the low levels of sequence identity, and the prominent structural differences from other SDR enzymes with known structures. The putative binding sites for the co-factor NADPH and the substrate (3R)-vestitone were defined and located in a large cleft formed between the N and C-terminal domains of enzyme. Potential key residues for enzyme activity were also identified, including the catalytic triad Ser129-Tyr164-Lys168. A molecular docking study showed that (3R)-vestitone, but not the (3S) isomer, forms favored interactions with the co-factor and catalytic triad, thus providing an explanation for the enzyme's strict substrate stereo-specificity.

About this Structure

2P4H is a Single protein structure of sequence from Medicago sativa. Full crystallographic information is available from OCA.

Reference

Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.)., Shao H, Dixon RA, Wang X, J Mol Biol. 2007 May 25;369(1):265-76. Epub 2007 Mar 21. PMID:17433362

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