|PROSITE documentation PDOC50972|
The ~250-residue pterin-binding domain has been shown to adopt a (β/α)8 barrel fold (see <PDB:1F6Y>), which has the overall shape of a distorted cylinder. It has eight α-helices stacked around the outside of an inner cylinder of parallel β-strands. The pterin ring binds at the bottom of the (β/α)8 barrel in a polar cup-like region that is relatively solvent exposed and fairly negatively charged. The pterin ring is partially buried within the (β/α)8 barrel. The pterin binding residues are highly conserved and include aspartate and asparagine residues located at the C-terminus of the β strands of the barrel, which are predicted to form hydrogen bonds with the nitrogen and oxygen atoms of the pterin ring [1,2,3].
Some proteins known to contain a pterin-binding domain are listed below:
The profile we developed covers the entire pterin-binding domain.Last update:
April 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Doukov T. Seravalli J. Stezowski J.J. Ragsdale S.W.|
|Title||Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.|
|2||Authors||Achari A. Somers D.O. Champness J.N. Bryant P.K. Rosemond J. Stammers D.K.|
|Title||Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase.|
|Source||Nat. Struct. Biol. 4:490-497(1997).|
|3||Authors||Evans J.C. Huddler D.P. Hilgers M.T. Romanchuk G. Matthews R.G. Ludwig M.L.|
|Title||Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 101:3729-3736(2004).|