5z49 | pdb_00005z49

Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose-1,5-bisphosphate

spinqualitylabelsall models 5z49, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5z49 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: RUB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CMPR_SYNE7] Activates transcription of the cmpABCD operon under carbon dioxide-limited conditions. Publication Abstract from PubMed The CO2-concentrating mechanism (CCM) has evolved to improve the efficiency of photosynthesis in autotrophic cyanobacteria. CmpR, a LysR-type transcriptional regulator (LTTR) from Synechococcus elongatus PCC 7942, was found to regulate CCM-related genes under low-CO2 conditions. Here, the dimeric structure of the effector-binding domain of CmpR (CmpR-EBD) in complex with the co-activator ribulose 1,5-bisphosphate (RuBP) is reported at 2.15 A resolution. One RuBP molecule binds to the inter-domain cleft between the two subunits of the CmpR-EBD dimer. Structural comparison combined with sequence analyses demonstrated that CmpR-EBD has an overall structure similar to those of LTTRs of known structure, but possesses a distinctly different effector-binding pattern. Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5-bisphosphate.,Mahounga DM, Sun H, Jiang YL Acta Crystallogr F Struct Biol Commun. 2018 Aug 1;74(Pt 8):506-511. doi:, 10.1107/S2053230X18008841. Epub 2018 Aug 1. PMID:30084400 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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