Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bock T, Kasten J, Muller R, Blankenfeldt W. Crystal structure of the HMG-CoA synthase MvaS from the Gram-negative bacterium Myxococcus xanthus. Chembiochem. 2016 Apr 28. doi: 10.1002/cbic.201600070. PMID:27124816 doi:http://dx.doi.org/10.1002/cbic.201600070
