5bst: Difference between revisions
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==Crystal structure of 4-coumarate:CoA ligase complexed with coumaroyl adenylate== | |||
<StructureSection load='5bst' size='340' side='right' caption='[[5bst]], [[Resolution|resolution]] 1.61Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5bst]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BST FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4UU:5-O-[(R)-HYDROXY{[(2E)-3-(4-OXOCYCLOHEXA-1,5-DIEN-1-YL)PROP-2-ENOYL]OXY}PHOSPHORYL]ADENOSINE'>4UU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bsm|5bsm]], [[5bsr|5bsr]], [[5bsu|5bsu]], [[5bsv|5bsv]], [[5bsw|5bsw]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-coumarate--CoA_ligase 4-coumarate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.12 6.2.1.12] </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=5bst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bst OCA], [http://pdbe.org/5bst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bst RCSB], [http://www.ebi.ac.uk/pdbsum/5bst PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plant 4-coumarate:CoA ligase (4CL) serves as a central catalyst in the phenylpropanoid pathway that provides precursors for numerous metabolites and regulates carbon flow. Here, we present several high-resolution crystal structures of Nicotiana tabacum 4CL isoform 2 (Nt4CL2) in complex with Mg(2+) and ATP, with AMP and coenzyme A (CoA), and with three different hydroxycinnamate-AMP intermediates: 4-coumaroyl-AMP, caffeoyl-AMP, and feruloyl-AMP. The Nt4CL2-Mg(2+)-ATP structure is captured in the adenylate-forming conformation, whereas the other structures are in the thioester-forming conformation. These structures represent a rare example of an ANL enzyme visualized in both conformations, and also reveal the binding determinants for both CoA and the hydroxycinnamate substrate. Kinetic studies of structure-based variants were used to identify residues crucial to catalysis, ATP binding, and hydroxycinnamate specificity. Lastly, we characterize a deletion mutant of Nt4CL2 that possesses the unusual sinapinate-utilizing activity. These studies establish a molecular framework for the engineering of this versatile biocatalyst. | |||
Structural Basis for Specificity and Flexibility in a Plant 4-Coumarate:CoA Ligase.,Li Z, Nair SK Structure. 2015 Nov 3;23(11):2032-42. doi: 10.1016/j.str.2015.08.012. Epub 2015, Sep 24. PMID:26412334<ref>PMID:26412334</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 5bst" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: 4-coumarate--CoA ligase]] | |||
[[Category: Li, Z]] | [[Category: Li, Z]] | ||
[[Category: Nair, S K]] | |||
[[Category: 4-coumarate:coa ligase]] | |||
[[Category: Ligase]] | |||
