1mlv

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Structure and Catalytic Mechanism of a SET Domain Protein MethyltransferaseStructure and Catalytic Mechanism of a SET Domain Protein Methyltransferase

Structural highlights

1mlv is a 3 chain structure with sequence from Pisum sativum. 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

Function

RBCMT_PEA Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase.[1]

Evolutionary Conservation

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

See Also

References

  1. Mininno M, Brugiere S, Pautre V, Gilgen A, Ma S, Ferro M, Tardif M, Alban C, Ravanel S. Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants. J Biol Chem. 2012 Jun 15;287(25):21034-44. doi: 10.1074/jbc.M112.359976. Epub, 2012 Apr 30. PMID:22547063 doi:http://dx.doi.org/10.1074/jbc.M112.359976

1mlv, resolution 2.60Å

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OCA