7cc3

Versatile cis-prenyltransferase MM_0014 from Methanosarcina mazei (crystal type: co-FG)

spinqualitylabelsall models 7cc3, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7cc3 is a 8 chain structure with sequence from Methanosarcina mazei Go1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.72Å Ligands: DPO, FQ0, FQF, FV3, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0F8R9A0_METMZ Publication Abstract from PubMed Polyprenyl groups, products of isoprenoid metabolism, are utilized in peptidoglycan biosynthesis, protein N-glycosylation, and other processes. These groups are formed by cis-prenyltransferases, which use allylic prenyl pyrophosphates as prenyl-donors to catalyze the C-prenylation of the general acceptor substrate, isopentenyl pyrophosphate. Repetition of this reaction forms (Z,E-mixed)-polyprenyl pyrophosphates, which are converted later into glycosyl carrier lipids, such as undecaprenyl phosphate and dolichyl phosphate. MM_0014 from the methanogenic archaeon Methanosarcina mazei is known as a versatile cis-prenyltransferase that accepts both isopentenyl pyrophosphate and dimethylallyl pyrophosphate as acceptor substrates. To learn more about this enzyme's catalytic activity, we determined the X-ray crystal structures of MM_0014 in the presence or absence of these substrates. Surprisingly, one structure revealed a complex with O-prenylglycerol, suggesting that the enzyme catalyzed the prenylation of glycerol contained in the crystallization buffer. Further analyses confirmed that the enzyme could catalyze the O-prenylation of small alcohols, such as 2-propanol, expanding our understanding of the catalytic ability of cis-prenyltransferases. A versatile cis-prenyltransferase from Methanosarcina mazei catalyzes both C- and O-prenylations.,Okada M, Unno H, Emi KI, Matsumoto M, Hemmi H J Biol Chem. 2021 Apr 16:100679. doi: 10.1016/j.jbc.2021.100679. PMID:33872599 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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