|PROSITE documentation PDOC50972
Pterin-binding domain profile
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:
- Prokaryotic and eukaryotic B12-dependent methionine synthase (MetH)
(EC 18.104.22.168), a large, modular protein that catalyzes the transfer of a
methyl group from methyltetrahydrofolate (CH3-H4folate) to Hcy to form
methionine, using cobalamin as an intermediate methyl carrier.
- Prokaryotic and eukaryotic dihydropteroate synthase (DHPS) (EC 22.214.171.124).
It catalyzes the condensation of para-aminobenzoic acid (pABA) with 7,8-
dihydropterin-pyrophosphate (DHPPP), eliminating pyrophosphate to form 7,8-
dihydropteroate which is subsequently converted to tetrahydrofolate.
- Moorella thermoacetica 5-methyltetrahydrofolate corrinoid/iron sulfur
protein methyltransferase (MeTr). It transfers the N5-methyl group from
CH3-H4folate to a cob(I)amide center in another protein, the corrinoid iron
The profile we developed covers the entire pterin-binding domain.
April 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|PTERIN_BINDING, PS50972; Pterin-binding domain profile (MATRIX)
|Sequences known to belong to this class detected by the profile:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1AD1 1AD4 1AJ0 1AJ2 ... [ALL]
||Doukov T., Seravalli J., Stezowski J.J., Ragsdale S.W.
||Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.
||Achari A., Somers D.O., Champness J.N., Bryant P.K., Rosemond J., Stammers D.K.
||Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase.
||Nat. Struct. Biol. 4:490-497(1997).
||Evans J.C., Huddler D.P., Hilgers M.T., Romanchuk G., Matthews R.G., Ludwig M.L.
||Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.
||Proc. Natl. Acad. Sci. U.S.A. 101:3729-3736(2004).
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