Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5-bisphosphate
| Autor: | Yong-Liang Jiang, Didel M Mahounga, Hui Sun |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Cyanobacteria Stereochemistry Dimer Ribulose-Bisphosphate Carboxylase 030106 microbiology Biophysics Biochemistry Protein Structure Secondary Research Communications 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Structural Biology Transcription (biology) Genetics Amino Acid Sequence Gene Ribulose 1 5-bisphosphate Binding Sites biology Effector Ribulose Condensed Matter Physics biology.organism_classification DNA-Binding Proteins 030104 developmental biology chemistry Crystallization Binding domain |
| Zdroj: | Acta Crystallogr F Struct Biol Commun |
| ISSN: | 2053-230X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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