5Z49

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

Summary for 5Z49

• Entry DOI: 10.2210/pdb5z49/pdb
• Descriptor: HTH-type transcriptional activator CmpR, RIBULOSE-1,5-DIPHOSPHATE (3 entities in total)
• Functional Keywords: transcription factor, cyanobacteria, transcription
• Biological source: Synechococcus elongatus PCC 7942 (Anacystis nidulans R2)
• Total number of polymer chains: 2
• Total formula weight: 52879.95

Authors

Jiang, Y.L.,Mahounga, D.M.,Sun, H. (deposition date: 2018-01-10, release date: 2018-10-10, Last modification date: 2023-11-22)

Primary citation

Mahounga, D.M.,Sun, H.,Jiang, Y.L.
Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5-bisphosphate.
Acta Crystallogr F Struct Biol Commun, 74:506-511, 2018

PubMed Abstract: The CO-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-CO 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 Å 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.

PubMed: 30084400
DOI: 10.1107/S2053230X18008841

Experimental method

X-RAY DIFFRACTION (2.148 Å)