Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus.

Authors :: Ren F
Feng X
Ko TP
Huang CH
Hu Y
Chan HC
Liu YL
Wang K
Chen CC
Pang X
He M
Li Y
Oldfield E
Guo RT
Source :: Chembiochem : a European journal of chemical biology [Chembiochem] 2013 Jan 21; Vol. 14 (2), pp. 195-9. Date of Electronic Publication: 2013 Jan 15.
Publication Year :: 2013
Abstract: Well structured: As a new triose phosphate isomerase (TIM) barrel-fold prenyl transferase, PcrB catalyzes the production of heptaprenylglyceryl phosphate from heptaprenyl diphosphate and glycerol-1-phosphate. Crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus in complex with ligands were solved, and together with site-directed mutagenesis and bioinformatics analyses, clearly reveal the catalytic mechanism of the enzyme.<br /> (Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Subjects :: Alkyl and Aryl Transferases genetics
Alkyl and Aryl Transferases metabolism
Bacillus subtilis chemistry
Bacillus subtilis genetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Conformation
Staphylococcus aureus chemistry
Staphylococcus aureus genetics
Triose-Phosphate Isomerase genetics
Triose-Phosphate Isomerase metabolism
Alkyl and Aryl Transferases chemistry
Bacillus subtilis enzymology
Staphylococcus aureus enzymology
Triose-Phosphate Isomerase chemistry

Full Text Access

Tools