Insights into TIM‐Barrel Prenyl Transferase Mechanisms: Crystal Structures of PcrB from Bacillus subtilis and Staphylococcus aureus. Issue 2 (15th January 2013)

• Record Type: Journal Article
• Authors: Ren, Feifei; Feng, Xinxin; Ko, Tzu‐Ping; Huang, Chun‐Hsiang; Hu, Yumei; Chan, Hsiu‐Chien; Liu, Yi‐Liang; Wang, Ke; Chen, Chun‐Chi; Pang, Xuefei; He, Miao; Li, Yujie; Oldfield, Eric; Guo, Rey‐Ting
• Is Part Of: Chembiochem. Volume 14:Issue 2(2013)
• Page Start: 195
• Page End: 199
• Publication Date: 2013-01-15
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201200748
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Well structured:</bold> 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 <italic>Bacillus subtilis</italic> and <italic>Staphylococcus aureus</italic> in complex with ligands were solved, and together with site‐directed mutagenesis and bioinformatics analyses, clearly reveal the catalytic mechanism of the enzyme.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1p8ft89r" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>