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- Title
Crystal structure of the effector‐binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5‐bisphosphate.
- Authors
Mahounga, Didel M.; Sun, Hui; Jiang, Yong-Liang
- Abstract
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 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.
- Subjects
CRYSTAL structure; SYNECHOCOCCUS elongatus; RIBULOSE bisphosphate carboxylase
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2018, Vol 74, Issue 8, p506
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X18008841