5hwp: Difference between revisions
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==MvaS with acetylated Cys115 in complex with coenzyme A== | |||
<StructureSection load='5hwp' size='340' side='right' caption='[[5hwp]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hwp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HWP 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_synthase Hydroxymethylglutaryl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.10 2.3.3.10] </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=5hwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hwp OCA], [http://pdbe.org/5hwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hwp RCSB], [http://www.ebi.ac.uk/pdbsum/5hwp PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A critical step in bacterial isoprenoid production is the synthesis of 3-hydroxy-3-methylglutaryl coenzyme A catalyzed by HMG-CoA synthase (HMGCS). In myxobacteria, this enzyme is also involved in a recently discovered acetyl-CoA-dependent isovaleryl-CoA biosynthesis pathway. Here we present crystal structures of MvaS, the HMGCS from Myxococcus xanthus, in complex with coenzyme A and acetylated active site Cys115, with the second substrate acetoacetyl-CoA and with the product 3-hydroxy-3-methylglutaryl-CoA. We show that MvaS uses the common HMGCS enzymatic mechanism and provide evidence that dimerization plays a role in the formation and stability of the active site. Overall, MvaS shows typical features of the eukaryotic HMGCS and exhibits differences to homologs from Gram-positive bacteria. This study provides insights into myxobacterial alternative isovaleryl coenzyme A biosynthesis and thereby extends the toolbox for the biotechnological production of renewable fuel and chemicals. | |||
Crystal structure of the HMG-CoA synthase MvaS from the Gram-negative bacterium Myxococcus xanthus.,Bock T, Kasten J, Muller R, Blankenfeldt W Chembiochem. 2016 Apr 28. doi: 10.1002/cbic.201600070. PMID:27124816<ref>PMID:27124816</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5hwp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hydroxymethylglutaryl-CoA synthase]] | |||
[[Category: Blankenfeldt, W]] | |||
[[Category: Bock, T]] | [[Category: Bock, T]] | ||
[[Category: Kasten, J]] | [[Category: Kasten, J]] | ||
[[Category: Biosynthesis]] | |||
[[Category: Mva]] | |||
[[Category: Myxococcus xanthus]] | |||
[[Category: Transferase]] | |||
