6UAK

LahSb - C-terminal methyltransferase involved in RiPP biosynthesis

Summary for 6UAK

• Entry DOI: 10.2210/pdb6uak/pdb
• Descriptor: SAM dependent methyltransferase LahSB, S-ADENOSYL-L-HOMOCYSTEINE (2 entities in total)
• Functional Keywords: methyltransferase, ripps, transferase
• Biological source: Lachnospiraceae bacterium C6A11
• Total number of polymer chains: 1
• Total formula weight: 35706.65

Authors

Nair, S.K.,Estrada, P. (deposition date: 2019-09-10, release date: 2019-12-04, Last modification date: 2024-03-13)

Primary citation

Huo, L.,Zhao, X.,Acedo, J.Z.,Estrada, P.,Nair, S.K.,van der Donk, W.A.
Characterization of a Dehydratase and Methyltransferase in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides in Lachnospiraceae.
Chembiochem, 21:190-199, 2020

PubMed Abstract: As a result of the exponential increase in genomic data, discovery of novel ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) has progressed rapidly in the past decade. The lanthipeptides are a major subset of RiPPs. Through genome mining we identified a novel lanthipeptide biosynthetic gene cluster (lah) from Lachnospiraceae bacterium C6A11, an anaerobic bacterium that is a member of the human microbiota and which is implicated in the development of host disease states such as type 2 diabetes and resistance to Clostridium difficile colonization. The lah cluster encodes at least seven putative precursor peptides and multiple post-translational modification (PTM) enzymes. Two unusual class II lanthipeptide synthetases LahM1/M2 and a substrate-tolerant S-adenosyl-l-methionine (SAM)-dependent methyltransferase LahS are biochemically characterized in this study. We also present the crystal structure of LahS in complex with product S-adenosylhomocysteine. This study sets the stage for further exploration of the final products of the lah pathway as well as their potential physiological functions in human/animal gut microbiota.

PubMed: 31532570
DOI: 10.1002/cbic.201900483

Experimental method

X-RAY DIFFRACTION (2.01 Å)