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Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogansCrystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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