7CAR

Versatile cis-prenyltransferase MM_0014 from Methanosarcina mazei (crystal type: free+IPP)

Summary for 7CAR

• Entry DOI: 10.2210/pdb7car/pdb
• Descriptor: cis-prenyltransferase, MM_0014, 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: cis-prenyltransferase, methanosarcina mazei, ipp, isoprenoid, mm_0014, archaea, transferase
• Biological source: Methanosarcina mazei Go1
• Total number of polymer chains: 2
• Total formula weight: 52069.44

Authors

Unno, H.,Hemmi, H. (deposition date: 2020-06-10, release date: 2021-04-28, Last modification date: 2023-11-29)

Primary citation

Okada, M.,Unno, H.,Emi, K.I.,Matsumoto, M.,Hemmi, H.
A versatile cis-prenyltransferase from Methanosarcina mazei catalyzes both C- and O-prenylations.
J.Biol.Chem., 296:100679-100679, 2021

PubMed Abstract: 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.

PubMed: 33872599
DOI: 10.1016/j.jbc.2021.100679

Experimental method

X-RAY DIFFRACTION (1.98 Å)