6LON
Crystal structure of HPSG
6LON の概要
| エントリーDOI | 10.2210/pdb6lon/pdb |
| 分子名称 | PFL2/glycerol dehydratase family glycyl radical enzyme, (2~{S})-2,3-bis(oxidanyl)propane-1-sulfonic acid, GLYCEROL, ... (5 entities in total) |
| 機能のキーワード | glycyl radical enzyme, dhps, c-s lyase., lyase |
| 由来する生物種 | Bilophila wadsworthia 3_1_6 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 382089.17 |
| 構造登録者 | |
| 主引用文献 | Liu, 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: 32571930DOI: 10.1073/pnas.2003434117 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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