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Crystal structure of the effector‐binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5‐bisphosphate
Author(s) -
Mahounga Didel M.,
Sun Hui,
Jiang Yong-Liang
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18008841
Subject(s) - effector , dimer , chemistry , synechococcus , photosynthesis , ribulose , regulator , biophysics , biochemistry , cyanobacteria , autotroph , biology , microbiology and biotechnology , rubisco , gene , genetics , bacteria , organic chemistry
The CO 2 ‐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 2 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.