2B5A
C.BclI, Control Element of the BclI Restriction-Modification System
Summary for 2B5A
Entry DOI | 10.2210/pdb2b5a/pdb |
Descriptor | C.BclI, ACETIC ACID (3 entities in total) |
Functional Keywords | helix-turn-helix motif, gene regulation |
Biological source | Bacillus caldolyticus |
Total number of polymer chains | 4 |
Total formula weight | 35845.43 |
Authors | Sawaya, M.R.,Zhu, Z.,Mersha, F.,Chan, S.H.,Dabur, R.,Xu, S.Y.,Balendiran, G.K. (deposition date: 2005-09-28, release date: 2006-01-03, Last modification date: 2024-02-14) |
Primary citation | Sawaya, M.R.,Zhu, Z.,Mersha, F.,Chan, S.H.,Dabur, R.,Xu, S.Y.,Balendiran, G.K. Crystal Structure of the Restriction-Modification System Control Element C.BclI and Mapping of Its Binding Site. Structure, 13:1837-1847, 2005 Cited by PubMed Abstract: Protection from DNA invasion is afforded by restriction-modification systems in many bacteria. The efficiency of protection depends crucially on the relative expression levels of restriction versus methytransferase genes. This regulation is provided by a controller protein, named C protein. Studies of the Bcll system in E. coli suggest that C.Bcll functions as a negative regulator for M.Bcll expression, implying that it plays a role in defense against foreign DNA during virus infection. C.Bcll binds (Kd = 14.3 nM) to a 2-fold symmetric C box DNA sequence that overlaps with the putative -35 promoter region upstream of the bcllM and bcllC genes. The C.Bcll fold comprises five alpha helices: two helices form a helix-turn-helix motif, and the remaining three helices form the extensive dimer interface. The C.Bcll-DNA model proposed suggests that DNA bending might play an important role in gene regulation, and that Glu27 and Asp31 in C.Bcll might function critically in the regulation. PubMed: 16338412DOI: 10.1016/j.str.2005.08.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.543 Å) |
Structure validation
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