4TR7: Crystal structure of DNA polymerase sliding clamp from Mycobaterium tuberculosis

Bacterial sliding clamps are molecular hubs that interact with many proteins involved in DNA metabolism through their binding, via a conserved peptidic sequence, into a universally conserved pocket. This interacting pocket is acknowledged as a potential molecular target for the development of new antibiotics. We previously designed short peptides with an improved affinity for the Escherichia coli binding pocket. Here we show that these peptides differentially interact with other bacterial clamps, despite the fact that all pockets are structurally similar. Thermodynamic and modeling analyses of the interactions differentiate between two categories of clamps: group I clamps interact efficiently with our designed peptides and assemble the Escherichia coli and related orthologs clamps, whereas group II clamps poorly interact with the same peptides and include Bacillus subtilis and other Gram-positive clamps. These studies also suggest that the peptide binding process could occur via different mechanisms, which depend on the type of clamp.
PDB ID: 4TR7Download
MMDB ID: 164170
PDB Deposition Date: 2014/6/14
Updated in MMDB: 2018/07
Experimental Method:
x-ray diffraction
Resolution: 2.29  Å
Source Organism:
Similar Structures:
Biological Unit for 4TR7: dimeric; determined by author and by software (PISA)
Molecular Components in 4TR7
Label Count Molecule
Proteins (2 molecules)
DNA Polymerase III Subunit Beta
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB