Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans.
Hou, X., Wang, Y., Zhou, Z., Bao, S., Lin, Y., Gong, W.(2007) J Struct Biol 159: 523-528
- PubMed: 17561415 
- DOI: https://doi.org/10.1016/j.jsb.2007.04.007
- Primary Citation of Related Structures:  
2HNK - PubMed Abstract: 
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.
Organizational Affiliation: 
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, PR China.