1wu8

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Crystal structure of project PH0463 from Pyrococcus horikoshii OT3Crystal structure of project PH0463 from Pyrococcus horikoshii OT3

Structural highlights

1wu8 is a 3 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

RSAMH_PYRHO Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM) into adenosine and L-methionine (PubMed:18551689). Is likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L-methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity). Probaly plays a role in preventing accumulation of (R)-S-adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L-methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases (By similarity). Is unable to mediate a fluorination or chlorination reaction with SAM (PubMed:18551689).[UniProtKB:A4X4S2][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Deng H, Botting CH, Hamilton JT, Russell RJ, O'Hagan D. S-adenosyl-L-methionine:hydroxide adenosyltransferase: a SAM enzyme. Angew Chem Int Ed Engl. 2008;47(29):5357-61. PMID:18551689 doi:10.1002/anie.200800794

1wu8, resolution 2.60Å

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