This title appears in the Scientific Report :
2009
Please use the identifier:
http://dx.doi.org/10.1074/jbc.M806591200 in citations.
Crystal structure of caseinolytic protease gene regulator, a transcriptional activator in actinomycetes
Crystal structure of caseinolytic protease gene regulator, a transcriptional activator in actinomycetes
Human pathogens of the genera Corynebacterium and Mycobacterium possess the transcriptional activator ClgR (clp gene regulator) which in Corynebacterium glutamicum has been shown to regulate the expression of the ClpCP protease genes. ClgR specifically binds to pseudo-palindromic operator regions up...
Saved in:
Personal Name(s): | Russo, S. |
---|---|
Schweitzer, J.-E. / Polen, T. / Bott, M. / Pohl, E. | |
Contributing Institute: |
Biotechnologie 1; IBT-1 |
Published in: | The @journal of biological chemistry, 284 (2009) S. 5208 - 5216 |
Imprint: |
Bethesda, Md.
Soc.
2009
|
Physical Description: |
5208 - 5216 |
PubMed ID: |
19019826 |
DOI: |
10.1074/jbc.M806591200 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Journal of Biological Chemistry
284 |
Subject (ZB): | |
Publikationsportal JuSER |
Human pathogens of the genera Corynebacterium and Mycobacterium possess the transcriptional activator ClgR (clp gene regulator) which in Corynebacterium glutamicum has been shown to regulate the expression of the ClpCP protease genes. ClgR specifically binds to pseudo-palindromic operator regions upstream of clpC and clpP1P2. Here, we present the first crystal structure of a ClgR protein from C. glutamicum. The structure was determined from two different crystal forms to resolutions of 1.75 and 2.05 A, respectively. ClgR folds into a five-helix bundle with a helix-turn-helix motif typical for DNA-binding proteins. Upon dimerization the two DNA-recognition helices are arranged opposite to each other at the protein surface in a distance of approximately 30 A, which suggests that they bind into two adjacent major grooves of B-DNA in an anti-parallel manner. A binding pocket is situated at a strategic position in the dimer interface and could possess a regulatory role altering the positions of the DNA-binding helices. |