PROSITE documentation PDOC50972Pterin-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 2.1.1.13), 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 2.5.1.15). 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 sulfur protein.
The profile we developed covers the entire pterin-binding domain.
Last update:April 2004 / First entry.
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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. | |
| Source | Structure 8:817-830(2000). | |
| PubMed ID | 10997901 |
| 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). | |
| PubMed ID | 9187658 |
| 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). | |
| PubMed ID | 14752199 | |
| DOI | 10.1073/pnas.0308082100 |
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