4TR8
Crystal structure of DNA polymerase sliding clamp from Pseudomonas aeruginosa
Summary for 4TR8
Entry DOI | 10.2210/pdb4tr8/pdb |
Descriptor | DNA polymerase III subunit beta, SODIUM ION (3 entities in total) |
Functional Keywords | dna polymerase, sliding clamp, processivity, dna binding protein |
Biological source | Pseudomonas aeruginosa HB15 |
Cellular location | Cytoplasm : V4MZL6 |
Total number of polymer chains | 2 |
Total formula weight | 85119.61 |
Authors | Olieric, V.,Burnouf, D.,Ennifar, E.,Wolff, P. (deposition date: 2014-06-15, release date: 2014-09-10, Last modification date: 2024-05-08) |
Primary citation | Wolff, P.,Amal, I.,Olieric, V.,Chaloin, O.,Gygli, G.,Ennifar, E.,Lorber, B.,Guichard, G.,Wagner, J.,Dejaegere, A.,Burnouf, D.Y. Differential Modes of Peptide Binding onto Replicative Sliding Clamps from Various Bacterial Origins. J.Med.Chem., 57:7565-7576, 2014 Cited by PubMed Abstract: 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. PubMed: 25170813DOI: 10.1021/jm500467a PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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