2hnk

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spinqualitylabelsall models 2hnk, resolution 2.300Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans

Overview

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 Structure

2HNK is a Single protein structure of sequence from Leptospira interrogans with , and as ligands. Full crystallographic information is available from OCA.

Reference

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 Apr 30;. PMID:17561415

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