Structural highlights
Function
[CMPR_SYNE7] Activates transcription of the cmpABCD operon under carbon dioxide-limited conditions.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Omata T, Gohta S, Takahashi Y, Harano Y, Maeda S. Involvement of a CbbR homolog in low CO2-induced activation of the bicarbonate transporter operon in cyanobacteria. J Bacteriol. 2001 Mar;183(6):1891-8. PMID:11222586 doi:http://dx.doi.org/10.1128/JB.183.6.1891-1898.2001
- ↑ Mahounga DM, Sun H, Jiang YL. Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5-bisphosphate. Acta Crystallogr F Struct Biol Commun. 2018 Aug 1;74(Pt 8):506-511. doi:, 10.1107/S2053230X18008841. Epub 2018 Aug 1. PMID:30084400 doi:http://dx.doi.org/10.1107/S2053230X18008841
