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PDBsum entry 1jql

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Top Page protein Protein-protein interface(s) links
Transferase PDB id
1jql
Contents
Protein chains
366 a.a. *
140 a.a. *
* Residue conservation analysis

References listed in PDB file
Key reference
Title Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of e. Coli DNA polymerase III.
Authors D.Jeruzalmi, O.Yurieva, Y.Zhao, M.Young, J.Stewart, M.Hingorani, M.O'Donnell, J.Kuriyan.
Ref. Cell, 2001, 106, 417-428. [DOI no: 10.1016/S0092-8674(01)00462-7]
PubMed id 11525728
Abstract
The dimeric ring-shaped sliding clamp of E. coli DNA polymerase III (beta subunit, homolog of eukaryotic PCNA) is loaded onto DNA by the clamp loader gamma complex (homolog of eukaryotic Replication Factor C, RFC). The delta subunit of the gamma complex binds to the beta ring and opens it. The crystal structure of a beta:delta complex shows that delta, which is structurally related to the delta' and gamma subunits of the gamma complex, is a molecular wrench that induces or traps a conformational change in beta such that one of its dimer interfaces is destabilized. Structural comparisons and molecular dynamics simulations suggest a spring-loaded mechanism in which the beta ring opens spontaneously once a dimer interface is perturbed by the delta wrench.
Figure 2.
Figure 2. Structure of the β:δ Complex(A) View along the edge of the β ring, centered on Domain 2 of β. (B) View showing the intermolecular interface involving Domain 3 of β. Structures shown in color are the β subunit and the δ subunit from the crystal structure of the complex. For reference, a second β monomer is shown in gray, taken from the crystal structure of the dimeric form of β (Kong et al., 1992), PDB code 2POL. The β-interaction element on δ (helix α4 and the loop following it) is colored yellow, and the side chains of two key hydrophobic residues of δ (Leu-73 and Phe-74) are shown
Figure 5.
Figure 5. Similarity in the Binding Modes of p21 and RB69 DNA Polymerase to the Interaction of δ with βThe structure of the β subunit in the β:δ complex is shown in gray and cyan. The structures of PCNA complexed to p21 (Gulbis et al., 1996) (PDB code 1AXC) and gp45 of RB69 complexed to a segment of RB69 DNA polymerase (Shamoo and Steitz, 1999) (PDB code 1B8H) were superimposed individually onto the structure of the β subunit by using the β strands at this interdomain interface to overlay the structures. The structure of the p21 peptide (orange) and the RB69 DNA polymerase tethering segment (yellow) are shown, but were not used in the structural superposition. The structure of δ is shown in green. PCNA and gp45 are not shown
The above figures are reprinted by permission from Cell Press: Cell (2001, 106, 417-428) copyright 2001.
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