Cover Picture: Insights into TIM‐Barrel Prenyl Transferase Mechanisms: Crystal Structures of PcrB from Bacillus subtilis and Staphylococcus aureus (ChemBioChem 2/2013). Issue 2 (17th January 2013)
- Record Type:
- Journal Article
- Title:
- Cover Picture: Insights into TIM‐Barrel Prenyl Transferase Mechanisms: Crystal Structures of PcrB from Bacillus subtilis and Staphylococcus aureus (ChemBioChem 2/2013). Issue 2 (17th January 2013)
- Main Title:
- Cover Picture: Insights into TIM‐Barrel Prenyl Transferase Mechanisms: Crystal Structures of PcrB from Bacillus subtilis and Staphylococcus aureus (ChemBioChem 2/2013)
- 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 - Abstract:
- <abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The cover picture shows</bold> the structure of the prenyl transferase PcrB. Prenyl transferases (PTs) play a key role in isoprenoid biosynthesis, and recently a new group of PTs with a triose phosphate isomerase (TIM)‐barrel fold have been discovered. The structures of PcrB from <italic>Bacillus subtilis</italic> and <italic>Staphylococcus aureus</italic> are reported here and show that there are two tyrosines and one glutamic acid in the active‐site region that are poised to activate the substrate's C3 OH group for nucleophilic attack, as well as remove H<sup>+</sup> from the active‐site region. The position of the prenyl diphosphate, which binds to an essential aspartic acid via Mg<sup>2+</sup>, was also located, and by using bioinformatics and site‐directed mutagenesis, a role for another tyrosine residue, in chain elongation, was demonstrated. In the article on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 195 ff., </ext-link> E. Oldfield, R.‐T. Guo et al. show how the results also provide a structural basis for the binding of a highly bent isoprenoid side chain in another TIM barrel PT, MoeO5.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1p8ft9cc" orientation="portrait" xlink:type="simple"<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The cover picture shows</bold> the structure of the prenyl transferase PcrB. Prenyl transferases (PTs) play a key role in isoprenoid biosynthesis, and recently a new group of PTs with a triose phosphate isomerase (TIM)‐barrel fold have been discovered. The structures of PcrB from <italic>Bacillus subtilis</italic> and <italic>Staphylococcus aureus</italic> are reported here and show that there are two tyrosines and one glutamic acid in the active‐site region that are poised to activate the substrate's C3 OH group for nucleophilic attack, as well as remove H<sup>+</sup> from the active‐site region. The position of the prenyl diphosphate, which binds to an essential aspartic acid via Mg<sup>2+</sup>, was also located, and by using bioinformatics and site‐directed mutagenesis, a role for another tyrosine residue, in chain elongation, was demonstrated. In the article on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 195 ff., </ext-link> E. Oldfield, R.‐T. Guo et al. show how the results also provide a structural basis for the binding of a highly bent isoprenoid side chain in another TIM barrel PT, MoeO5.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1p8ft9cc" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract> … (more)
- Is Part Of:
- Chembiochem. Volume 14:Issue 2(2013)
- Journal:
- Chembiochem
- Issue:
- Volume 14:Issue 2(2013)
- Issue Display:
- Volume 14, Issue 2 (2013)
- Year:
- 2013
- Volume:
- 14
- Issue:
- 2
- Issue Sort Value:
- 2013-0014-0002-0000
- Page Start:
- 165
- Page End:
- 165
- Publication Date:
- 2013-01-17
- Subjects:
- Biochemistry -- Periodicals
Molecular biology -- Periodicals
Pharmaceutical chemistry -- Periodicals
572 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1439-7633 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cbic.201390000 ↗
- Languages:
- English
- ISSNs:
- 1439-4227
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3133.490980
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3528.xml