3wgg | pdb_00003wgg

Crystal structure of RSP in complex with alpha-NAD+

spinqualitylabelsall models 3wgg, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wgg is a 2 chain structure with sequence from Thermoanaerobacter ethanolicus JW 200. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: 8NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D5KM69_THEET Modulates transcription in response to changes in cellular NADH/NAD(+) redox state (By similarity).[HAMAP-Rule:MF_01131][SAAS:SAAS003781_004_005573] Publication Abstract from PubMed 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/alpha-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 alpha8. Consequently, the RSP dimer may be locked in a closed conformation that does not bind to DNA. However, alpha-NAD(+) does not show a higher affinity to RSP than beta-NAD(+). It has to be improved for possible use as an effector in modulating the repressor. Binding mode of the oxidized alpha-anomer of NAD(+) to RSP, a Rex-family repressor.,Zheng Y, Ko TP, Yang Y, Shao W, Guo RT Biochem Biophys Res Commun. 2015 Jan 16;456(3):733-6. doi:, 10.1016/j.bbrc.2014.12.049. Epub 2014 Dec 16. PMID:25527330 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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