کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2829301 | 1162800 | 2007 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans](/preview/png/2829301.png)
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.
Journal: Journal of Structural Biology - Volume 159, Issue 3, September 2007, Pages 523–528