3F52: Crystal Structure Of The Clp Gene Regulator Clgr From C. Glutamicum

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.
PDB ID: 3F52Download
MMDB ID: 68046
PDB Deposition Date: 2008/11/3
Updated in MMDB: 2008/11
Experimental Method:
x-ray diffraction
Resolution: 1.75  Å
Source Organism:
Similar Structures:
Biological Unit for 3F52: dimeric; determined by author and by software (PISA)
Molecular Components in 3F52
Label Count Molecule
Proteins (2 molecules)
CLP Gene Regulator (Clgr)
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

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