2HNK

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

Summary for 2HNK

• Entry DOI: 10.2210/pdb2hnk/pdb
• Descriptor: SAM-dependent O-methyltransferase, SULFATE ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (5 entities in total)
• Functional Keywords: modified rossman fold, transferase
• Biological source: Leptospira interrogans
• Total number of polymer chains: 3
• Total formula weight: 82864.93

Authors

Hou, X.,Wei, Z.,Gong, W. (deposition date: 2006-07-13, release date: 2007-09-04, Last modification date: 2024-03-13)

Primary citation

Hou, X.,Wang, Y.,Zhou, Z.,Bao, S.,Lin, Y.,Gong, W.
Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans.
J.Struct.Biol., 159:523-528, 2007

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.

PubMed: 17561415
DOI: 10.1016/j.jsb.2007.04.007

Experimental method

X-RAY DIFFRACTION (2.3 Å)