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6LON

Crystal structure of HPSG

Summary for 6LON
Entry DOI10.2210/pdb6lon/pdb
DescriptorPFL2/glycerol dehydratase family glycyl radical enzyme, (2~{S})-2,3-bis(oxidanyl)propane-1-sulfonic acid, GLYCEROL, ... (5 entities in total)
Functional Keywordsglycyl radical enzyme, dhps, c-s lyase., lyase
Biological sourceBilophila wadsworthia 3_1_6
Total number of polymer chains4
Total formula weight382089.17
Authors
Liu, J.,Zhang, Y.,Yuchi, Z. (deposition date: 2020-01-06, release date: 2020-06-24, Last modification date: 2023-11-29)
Primary citationLiu, J.,Wei, Y.,Lin, L.,Teng, L.,Yin, J.,Lu, Q.,Chen, J.,Zheng, Y.,Li, Y.,Xu, R.,Zhai, W.,Liu, Y.,Liu, Y.,Cao, P.,Ang, E.L.,Zhao, H.,Yuchi, Z.,Zhang, Y.
Two radical-dependent mechanisms for anaerobic degradation of the globally abundant organosulfur compound dihydroxypropanesulfonate.
Proc.Natl.Acad.Sci.USA, 117:15599-15608, 2020
Cited by
PubMed Abstract: 2()-dihydroxypropanesulfonate (DHPS) is a microbial degradation product of 6-deoxy-6-sulfo-d-glucopyranose (sulfoquinovose), a component of plant sulfolipid with an estimated annual production of 10 tons. DHPS is also at millimolar levels in highly abundant marine phytoplankton. Its degradation and sulfur recycling by microbes, thus, play important roles in the biogeochemical sulfur cycle. However, DHPS degradative pathways in the anaerobic biosphere are not well understood. Here, we report the discovery and characterization of two O-sensitive glycyl radical enzymes that use distinct mechanisms for DHPS degradation. DHPS-sulfolyase (HpsG) in sulfate- and sulfite-reducing bacteria catalyzes C-S cleavage to release sulfite for use as a terminal electron acceptor in respiration, producing HS. DHPS-dehydratase (HpfG), in fermenting bacteria, catalyzes C-O cleavage to generate 3-sulfopropionaldehyde, subsequently reduced by the NADH-dependent sulfopropionaldehyde reductase (HpfD). Both enzymes are present in bacteria from diverse environments including human gut, suggesting the contribution of enzymatic radical chemistry to sulfur flux in various anaerobic niches.
PubMed: 32571930
DOI: 10.1073/pnas.2003434117
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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