3WGG
Crystal structure of RSP in complex with alpha-NAD+
Summary for 3WGG
| Entry DOI | 10.2210/pdb3wgg/pdb |
| Related | 3WG9 3WGH 3WGI |
| Descriptor | Redox-sensing transcriptional repressor rex, alpha-Diphosphopyridine nucleotide, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | winged helix, rossmann fold, transcription repressor, transcription |
| Biological source | Thermoanaerobacter ethanolicus |
| Cellular location | Cytoplasm : D5KM69 |
| Total number of polymer chains | 2 |
| Total formula weight | 52851.79 |
| Authors | Zheng, Y.,Ko, T.-P.,Guo, R.-T. (deposition date: 2013-08-05, release date: 2014-08-13, Last modification date: 2023-11-08) |
| Primary citation | Zheng, Y.,Ko, T.-P.,Yang, Y.,Shao, W.,Guo, R.-T. Binding mode of the oxidized alpha-anomer of NAD(+) to RSP, a Rex-family repressor Biochem.Biophys.Res.Commun., 456:733-736, 2015 Cited by PubMed Abstract: The Rex-family repressors sense redox levels by alternative binding to NADH or NAD(+). RSP is the homologue of Rex in Thermoanaerobacter ethanolicus JW200(T) and regulates ethanol fermentation in this obligate anaerobe. The dimeric repressor binds to DNA by an open conformation. The crystal structure of RSP/α-NAD(+) complex shows a different set of ligand interactions mainly due to the unique configuration of the nicotinamide moiety. The positively charged ring is covered by the Tyr102 side chain and interacts with a sulfate ion adjacent to the N-terminus of helix α8. Consequently, the RSP dimer may be locked in a closed conformation that does not bind to DNA. However, α-NAD(+) does not show a higher affinity to RSP than β-NAD(+). It has to be improved for possible use as an effector in modulating the repressor. PubMed: 25527330DOI: 10.1016/j.bbrc.2014.12.049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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