6e1j
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Methylthioalkylmalate Synthase (BjuMAM1.1) from Brassica juncea== | |
| + | <StructureSection load='6e1j' size='340' side='right'caption='[[6e1j]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6e1j]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E1J FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=KMT:4-(METHYLSULFANYL)-2-OXOBUTANOIC+ACID'>KMT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=6e1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e1j OCA], [http://pdbe.org/6e1j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e1j RCSB], [http://www.ebi.ac.uk/pdbsum/6e1j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e1j ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Methylthioalkylmalate synthase catalyzes the committed step in the side-chain elongation of methionine-derived aliphatic glucosinolates and likely evolved from the isopropylmalate synthases of leucine biosynthesis. The globally cultivated Brassica species possess diverse aliphatic glucosinolates important for plant defense and animal nutrition; however, the molecular basis for the evolution of methylthioalkylmalate synthase and its generation of natural product diversity in Brassica is poorly understood. Here we show that Brassica genomes encode multiple methylthioalkylmalate synthase that have differences in expression profiles and 2-oxo substrate preference that account for diversity of aliphatic glucosinolates across Brassica accessions. The 2.1 A resolution x-ray crystal structure of B. juncea methylthioalkylmalate synthase identifies key active site residues responsible for controlling specificity for different 2-oxo substrates and the determinants of side-chain length in aliphatic glucosinolates. Overall, these results provide the evolutionary and biochemical foundation for diversification of glucosinolates profiles across globally-cultivated Brassica species, which could be used with ongoing breeding strategies towards manipulation of beneficial glucosinolates compounds for animal health and plant protection. | ||
| - | + | Molecular Basis of the Evolution of Methylthioalkylmalate Synthase and Diversity of Methionine-Derived Glucosinolates.,Kumar R, Lee SG, Augustine R, Reichelt M, Vassao DG, Palavalli MH, Allen A, Gershenzon J, Jez JM, Bisht NC Plant Cell. 2019 Apr 25. pii: tpc.19.00046. doi: 10.1105/tpc.19.00046. PMID:31023839<ref>PMID:31023839</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Lee, S | + | <div class="pdbe-citations 6e1j" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jez, J M]] | ||
| + | [[Category: Lee, S G]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Methylthioalkylmalate synthase]] | ||
| + | [[Category: Plant protein]] | ||
| + | [[Category: X-ray crystal structure]] | ||
Revision as of 11:16, 10 May 2019
Crystal Structure of Methylthioalkylmalate Synthase (BjuMAM1.1) from Brassica juncea
| |||||||||||
