5YMR

The Crystal Structure of IseG

Summary for 5YMR

• Entry DOI: 10.2210/pdb5ymr/pdb
• Descriptor: Formate acetyltransferase, 2-hydroxyethylsulfonic acid, GLYCEROL, ... (4 entities in total)
• Functional Keywords: isethionate, glycyl radical enzyme, c-s bond cleavage, lyase
• Biological source: Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
• Total number of polymer chains: 4
• Total formula weight: 366915.00

Authors

Lin, L.,Zhang, J.,Xing, M.,Hua, G.,Guo, C.,Hu, Y.,Wei, Y.,Ang, E.,Zhao, H.,Zhang, Y.,Yuchi, Z. (deposition date: 2017-10-22, release date: 2019-03-20, Last modification date: 2024-03-27)

Primary citation

Xing, M.,Wei, Y.,Zhou, Y.,Zhang, J.,Lin, L.,Hu, Y.,Hua, G.,N Nanjaraj Urs, A.,Liu, D.,Wang, F.,Guo, C.,Tong, Y.,Li, M.,Liu, Y.,Ang, E.L.,Zhao, H.,Yuchi, Z.,Zhang, Y.
Radical-mediated C-S bond cleavage in C2 sulfonate degradation by anaerobic bacteria.
Nat Commun, 10:1609-1609, 2019

PubMed Abstract: Bacterial degradation of organosulfonates plays an important role in sulfur recycling, and has been extensively studied. However, this process in anaerobic bacteria especially gut bacteria is little known despite of its potential significant impact on human health with the production of toxic HS. Here, we describe the structural and biochemical characterization of an oxygen-sensitive enzyme that catalyzes the radical-mediated C-S bond cleavage of isethionate to form sulfite and acetaldehyde. We demonstrate its involvement in pathways that enables C2 sulfonates to be used as terminal electron acceptors for anaerobic respiration in sulfate- and sulfite-reducing bacteria. Furthermore, it plays a key role in converting bile salt-derived taurine into HS in the disease-associated gut bacterium Bilophila wadsworthia. The enzymes and transporters in these anaerobic pathways expand our understanding of microbial sulfur metabolism, and help deciphering the complex web of microbial pathways involved in the transformation of sulfur compounds in the gut.

PubMed: 30962433
DOI: 10.1038/s41467-019-09618-8

Experimental method

X-RAY DIFFRACTION (2.4 Å)