2p4h

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(Difference between revisions)

Revision as of 13:50, 10 September 2015

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

Structural highlights

2p4h is a 1 chain structure with sequence from Alfalfa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Vestitone Reductase (Alfalfa)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[VESTR_MEDSA] Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Guo L, Paiva NL. Molecular cloning and expression of alfalfa (Medicago sativa L.) vestitone reductase, the penultimate enzyme in medicarpin biosynthesis. Arch Biochem Biophys. 1995 Jul 10;320(2):353-60. PMID:7625843
↑ Guo L, Dixon RA, Paiva NL. The 'pterocarpan synthase' of alfalfa: association and co-induction of vestitone reductase and 7,2'-dihydroxy-4'-methoxy-isoflavanol (DMI) dehydratase, the two final enzymes in medicarpin biosynthesis. FEBS Lett. 1994 Dec 19;356(2-3):221-5. PMID:7805842
↑ Guo L, Dixon RA, Paiva NL. Conversion of vestitone to medicarpin in alfalfa (Medicago sativa L.) is catalyzed by two independent enzymes. Identification, purification, and characterization of vestitone reductase and 7,2'-dihydroxy-4'-methoxyisoflavanol dehydratase. J Biol Chem. 1994 Sep 2;269(35):22372-8. PMID:8071365
↑ Shao H, Dixon RA, Wang X. Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.). J Mol Biol. 2007 May 25;369(1):265-76. Epub 2007 Mar 21. PMID:17433362 doi:10.1016/j.jmb.2007.03.040

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p4h"

@@ Line 2: / Line 2: @@
 <StructureSection load='2p4h' size='340' side='right' caption='[[2p4h]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2p4h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P4H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2p4h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P4H FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vestitone Reductase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3879 Medicago sativa])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vestitone Reductase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3879 Alfalfa])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p4h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p4h RCSB], [http://www.ebi.ac.uk/pdbsum/2p4h PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p4h OCA], [http://pdbe.org/2p4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p4h RCSB], [http://www.ebi.ac.uk/pdbsum/2p4h PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/VESTR_MEDSA VESTR_MEDSA]] Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions.<ref>PMID:7625843</ref> <ref>PMID:7805842</ref> <ref>PMID:8071365</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 24: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2p4h" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Medicago sativa]]
+[[Category: Alfalfa]]
 [[Category: Dixon, R A]]
 [[Category: Shao, H]]

2p4h

From Proteopedia

Revision as of 13:50, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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