1fpq

From Proteopedia

(Difference between revisions)

Revision as of 09:31, 27 December 2017

CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE

Structural highlights

1fpq 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.
Ligands:
NonStd Res:
Related:	1fp1, 1fp2, 1fpx
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CHOMT_MEDSA] Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.^[1] ^[2]

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

Chalcone O-methyltransferase (ChOMT) and isoflavone O-methyltransferase (IOMT) are S-adenosyl-l-methionine (SAM) dependent plant natural product methyltransferases involved in secondary metabolism in Medicago sativa (alfalfa). Here we report the crystal structure of ChOMT in complex with the product S-adenosyl-l-homocysteine and the substrate isoliquiritigenin (4,2',4'-trihydroxychalcone) refined to 1.8 A as well as the crystal structure of IOMT in complex with the products S-adenosyl-l-homocysteine and isoformononetin (4'-hydroxy-7-methoxyisoflavone) refined to 1.4 A. These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection. As such, this work provides a structural basis for understanding the substrate specificity of the diverse family of plant OMTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes.

Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.,Zubieta C, He XZ, Dixon RA, Noel JP Nat Struct Biol. 2001 Mar;8(3):271-9. PMID:11224575^[3]

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

References

↑ Maxwell CA, Edwards R, Dixon RA. Identification, purification, and characterization of S-adenosyl-L-methionine: isoliquiritigenin 2'-O-methyltransferase from alfalfa (Medicago sativa L.). Arch Biochem Biophys. 1992 Feb 14;293(1):158-66. PMID:1731632
↑ Ichimura M, Furuno T, Takahashi T, Dixon RA, Ayabe S. Enzymic O-methylation of isoliquiritigenin and licodione in alfalfa and licorice cultures. Phytochemistry. 1997 Mar;44(6):991-5. PMID:9055445
↑ Zubieta C, He XZ, Dixon RA, Noel JP. Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nat Struct Biol. 2001 Mar;8(3):271-9. PMID:11224575 doi:http://dx.doi.org/10.1038/85029

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/1fpq"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE==
 <StructureSection load='1fpq' size='340' side='right' caption='[[1fpq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fp1|1fp1]], [[1fp2|1fp2]], [[1fpx|1fpx]]</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=1fpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpq OCA], [http://pdbe.org/1fpq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fpq RCSB], [http://www.ebi.ac.uk/pdbsum/1fpq 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=1fpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpq OCA], [http://pdbe.org/1fpq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fpq RCSB], [http://www.ebi.ac.uk/pdbsum/1fpq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1fpq

From Proteopedia

Revision as of 09:31, 27 December 2017

CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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