2hnk
Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans
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| , resolution 2.300Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
The S-adenosylmethionine (SAM)-dependent O-methyltransferase from Leptospira interrogans (LiOMT) expressed by gene LA0415 belongs to the Methyltransf_3 family (Pfam PF01596). In this family all of the five bacterial homologues with known function are reported as SAM-dependent O-methylstransferases involved in antibiotic production. The crystal structure of LiOMT in complex with S-adenosylhomocysteine reported here is the first bacterial protein structure in this family. The LiOMT structure shows a conserved SAM-binding region and a probable metal-dependent catalytic site. The molecules of LiOMT generate homodimers by N-terminal swapping, which assists the pre-organization of the substrate-binding site. Based on the sequence and structural analysis, it is implied by the catalytic and substrate-binding site that the substrate of LiOMT is a phenolic derivative, which probably has a large ring-shaped moiety.
About this StructureAbout this Structure
2HNK is a Single protein structure of sequence from Leptospira interrogans. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans., Hou X, Wang Y, Zhou Z, Bao S, Lin Y, Gong W, J Struct Biol. 2007 Sep;159(3):523-8. Epub 2007 Apr 30. PMID:17561415
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