7CM9
DMSP lyase DddX
Summary for 7CM9
| Entry DOI | 10.2210/pdb7cm9/pdb |
| Descriptor | DMSP lyase, ADENOSINE-5'-TRIPHOSPHATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | atp-dependent dmsp lyase, lyase |
| Biological source | Psychrobacter sp. |
| Total number of polymer chains | 4 |
| Total formula weight | 329195.54 |
| Authors | Li, C.Y.,Zhang, Y.Z. (deposition date: 2020-07-25, release date: 2021-05-19, Last modification date: 2024-03-27) |
| Primary citation | Li, C.Y.,Wang, X.J.,Chen, X.L.,Sheng, Q.,Zhang, S.,Wang, P.,Quareshy, M.,Rihtman, B.,Shao, X.,Gao, C.,Li, F.,Li, S.,Zhang, W.,Zhang, X.H.,Yang, G.P.,Todd, J.D.,Chen, Y.,Zhang, Y.Z. A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA. Elife, 10:-, 2021 Cited by PubMed Abstract: Dimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule in marine environments with important roles in global sulfur and nutrient cycling. Diverse DMSP lyases in some algae, bacteria, and fungi cleave DMSP to yield gaseous dimethyl sulfide (DMS), an infochemical with important roles in atmospheric chemistry. Here, we identified a novel ATP-dependent DMSP lyase, DddX. DddX belongs to the acyl-CoA synthetase superfamily and is distinct from the eight other known DMSP lyases. DddX catalyses the conversion of DMSP to DMS via a two-step reaction: the ligation of DMSP with CoA to form the intermediate DMSP-CoA, which is then cleaved to DMS and acryloyl-CoA. The novel catalytic mechanism was elucidated by structural and biochemical analyses. DddX is found in several Alphaproteobacteria, Gammaproteobacteria, and Firmicutes, suggesting that this new DMSP lyase may play an overlooked role in DMSP/DMS cycles. PubMed: 33970104DOI: 10.7554/eLife.64045 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.249 Å) |
Structure validation
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