Insights into TIM‐Barrel Prenyl Transferase Mechanisms: Crystal Structures of PcrB from Bacillus subtilis and Staphylococcus aureus

• DOI: 10.1002/cbic.201200748
• Publication Date: 2013-01-15T21:05:51Z
• Authors: Feifei Ren; Xinxin Feng; Tzu‐Ping Ko; Chun‐Hsiang Huang; Yumei Hu; Hsiu‐Chien Chan; Yi‐Liang Liu; Ke Wang; Chun‐Chi Chen; Xuefei Pang; Miao He; Yujie Li; Eric Oldfield; Rey‐Ting Guo
• Keywords: Models, Molecular; 0301 basic medicine; Staphylococcus aureus; 03 medical and health sciences; Alkyl and Aryl Transferases; Protein Conformation; Mutagenesis, Site-Directed; Bacillus subtilis; Triose-Phosphate Isomerase; 3. Good health

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.