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

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.

SUBMITTER: Ren F

PROVIDER: S-EPMC3769695 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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

Ren Feifei F Feng Xinxin X Ko Tzu-Ping TP Huang Chun-Hsiang CH Hu Yumei Y Chan Hsiu-Chien HC Liu Yi-Liang YL Wang Ke K Chen Chun-Chi CC Pang Xuefei X He Miao M Li Yujie Y Oldfield Eric E Guo Rey-Ting RT

Chembiochem : a European journal of chemical biology 20130115 2

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. ...[more]

PMID: 23322418

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