This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fpx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (04:55, 8 March 2018) (edit) (undo)
(Redirecting to 6cig)
 
Line 1: Line 1:
-
 
+
#REDIRECT [[6cig]] This PDB entry is obsolete and replaced by 6cig
-
==CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED ISOFLAVONE O-METHYLTRANSFERASE==
+
-
<StructureSection load='1fpx' size='340' side='right' caption='[[1fpx]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+
-
== Structural highlights ==
+
-
<table><tr><td colspan='2'>[[1fpx]] 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=1FPX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FPX FirstGlance]. <br>
+
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
+
-
<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]], [[1fpq|1fpq]]</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=1fpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpx OCA], [http://pdbe.org/1fpx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fpx RCSB], [http://www.ebi.ac.uk/pdbsum/1fpx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpx ProSAT]</span></td></tr>
+
-
</table>
+
-
== Function ==
+
-
[[http://www.uniprot.org/uniprot/7OMT8_MEDSA 7OMT8_MEDSA]] Transfers a methyl group to 7-hydroxyls of the isoflavones daidzein, genistein and 6,7,4'-trihydroxyisoflavone. Can also methylate (+)6a-hydroxymaackiain with lower efficiency.
+
-
== Evolutionary Conservation ==
+
-
[[Image:Consurf_key_small.gif|200px|right]]
+
-
Check<jmol>
+
-
<jmolCheckbox>
+
-
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpx_consurf.spt"</scriptWhenChecked>
+
-
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+
-
<text>to colour the structure by Evolutionary Conservation</text>
+
-
</jmolCheckbox>
+
-
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fpx ConSurf].
+
-
<div style="clear:both"></div>
+
-
<div style="background-color:#fffaf0;">
+
-
== 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<ref>PMID:11224575</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 1fpx" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
-
__TOC__
+
-
</StructureSection>
+
-
[[Category: Alfalfa]]
+
-
[[Category: Dixon, R A]]
+
-
[[Category: Noel, J P]]
+
-
[[Category: Zubieta, C]]
+
-
[[Category: S-adenosymethionine complex]]
+
-
[[Category: Selenomethionine]]
+
-
[[Category: Transferase]]
+

Current revision

  1. REDIRECT 6cig This PDB entry is obsolete and replaced by 6cig

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools