5A0U
Structure of CutC choline lyase choline bound form from Klebsiella pneumoniae.
Summary for 5A0U
| Entry DOI | 10.2210/pdb5a0u/pdb |
| Descriptor | CHOLINE TRIMETHYLAMINE LYASE, CHOLINE ION (3 entities in total) |
| Functional Keywords | lyase, cutc, choline tma lyase, glycyl radical enzyme |
| Biological source | KLEBSIELLA PNEUMONIAE |
| Total number of polymer chains | 8 |
| Total formula weight | 716648.74 |
| Authors | Kalnins, G.,Tars, K. (deposition date: 2015-04-23, release date: 2015-07-29, Last modification date: 2024-01-10) |
| Primary citation | Kalnins, G.,Kuka, J.,Grinberga, S.,Makrecka-Kuka, M.,Liepinsh, E.,Dambrova, M.,Tars, K. Structure and Function of Cutc Choline Lyase from Human Microbiota Bacterium Klebsiella Pneumoniaee J.Biol.Chem., 290:21732-, 2015 Cited by PubMed Abstract: CutC choline trimethylamine-lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde. In humans, TMA is produced exclusively by the intestinal microbiota, and its metabolite, trimethylamine oxide, has been associated with a higher risk of cardiovascular diseases. Therefore, information about the three-dimensional structures of TMA-producing enzymes is important for microbiota-targeted drug discovery. We have cloned, expressed, and purified the CutC GRE and the activating enzyme CutD from Klebsiella pneumoniae, a representative of the human microbiota. We have determined the first crystal structures of both the choline-bound and choline-free forms of CutC and have discovered that binding of choline at the ligand-binding site triggers conformational changes in the enzyme structure, a feature that has not been observed for any other characterized GRE. PubMed: 26187464DOI: 10.1074/JBC.M115.670471 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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