Pt-barrel
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The PT-barrel, is a new protein fold.
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[edit] The PT-Barrel Fold
It consists of a closed β-sheet comprising ten anti-parallel β-strands arranged around a central β-barrel core, itself surrounded by a ring of α-helices forming the outer, solvent exposed surface of the barrel.
The secondary connectivity nearly conforms to an (ααββ)5 classification, but is more specifically described using the (ααββ)4-(αββ)−α nomenclature, where helices 6 and 8, both involved in inter-protein contacts in the crystal lattice, display a helical “kink”. The most hydrophobic section of the PT-barrel is the region residing between the outer surface of the cylindrical β-barrel and the belt of surrounding α-helices. Additionally, a number of hydrophobic residues located inside the barrel accommodate the prenyl tail of the Geranyl-diPhosphate (GPP) and GSPP molecules, while the diphosphate or the thio-diphosphate head groups of substrate and substrate analogs, respectively, point toward the “upper”, more polar end of the barrel where a Mg2+ ion is coordinated. Finally, the bottom of the barrel is capped by a short C-terminal helix (α11).
[edit] References
- Kuzuyama T, Noel JP, Richard SB. Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products. Nature. 2005 Jun 16;435(7044):983-7.
- Koehl P. Relaxed specificity in aromatic prenyltransferases. Nat Chem Biol. 2005 Jul;1(2):71-2.
- Botta B, Delle Monache G, Menendez P, Boffi A. Novel prenyltransferase enzymes as a tool for flavonoid prenylation. Trends Pharmacol Sci. 2005 Dec;26(12):606-8. Epub 2005 Oct 17.
[edit] Online Resources
The PT-Barrel Ressource is under construction
[edit] Press Releases
Promiscuous Catalytic Activity Possessed by Novel Enzyme Structure, June 15, 2005
SSRL Science Highlight July 2005
LightSource.org Press Release Number: PR-SSRL-05-3
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