scholarly journals The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unique quarternary assembly

2007 ◽  
Vol 69 (3) ◽  
pp. 679-682 ◽  
Author(s):  
Pavlína Řezáčová ◽  
Veronika Krejčiříková ◽  
Dominika Borek ◽  
Shiu F. Moy ◽  
Andrzej Joachimiak ◽  
...  
2019 ◽  
Vol 64 (7) ◽  
pp. 1126-1133 ◽  
Author(s):  
A. Nayab ◽  
S. A. Moududee ◽  
Y. Shi ◽  
Y. Jiang ◽  
Q. Gong

Author(s):  
Didel M. Mahounga ◽  
Hui Sun ◽  
Yong-Liang Jiang

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.


2010 ◽  
Vol 400 (5) ◽  
pp. 998-1010 ◽  
Author(s):  
Misty D. Balcewich ◽  
Thomas M. Reeve ◽  
Evan A. Orlikow ◽  
Lynda J. Donald ◽  
David J. Vocadlo ◽  
...  

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