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PDBsum entry 1a5t

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Zinc finger PDB id
1a5t
Contents
Protein chain
324 a.a.
Metals
_ZN
Waters ×606

References listed in PDB file
Key reference
Title Crystal structure of the delta' Subunit of the clamp-Loader complex of e. Coli DNA polymerase III.
Authors B.Guenther, R.Onrust, A.Sali, M.O'Donnell, J.Kuriyan.
Ref. Cell, 1997, 91, 335-345. [DOI no: 10.1016/S0092-8674(00)80417-1]
PubMed id 9363942
Abstract
The crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III has been determined. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site. The catalytic component of the clamp-loader complex is the gamma subunit, which is homologous to delta'. A sequence-structure alignment suggests that nucleotides bind to gamma at an interdomain interface within the inner surface of the "C." The alignment is extended to other clamp-loader complexes and to the RuvB family of DNA helicases, and suggests that each of these is assembled from C-shaped components that can open and close the jaws of the "C" in response to ATP binding and hydrolysis.
Figure 5.
Figure 5. Inactive Nucleotide-Binding Region of δ′The region surrounding the P loop of δ′ is shown, with side chains of certain residues indicated in stick representation. P-loop sequences and sensor sequences in δ′ and other proteins are indicated. The structure of ATP is taken from adenylate kinase, after the P-loop segments of adenylate kinase and δ′ were superimposed. Residues that are actual or potential ligands of the phosphate groups of ATP are highlighed in blue in the alignment of sequence motifs.
Figure 6.
Figure 6. GRASP Diagrams of δ′The molecular surface of δ′ is shown in two orientations, colored according to local electrostatic potential. A transparent representation of the surface with the polypeptide backbone revealed underneath is also shown. Note that there are no contacts between Domains 1 and 3, and that the appearance of such contacts in the GRASP diagram is a consequence of the orientation of the molecule. Figure prepared using GRASP ([32]).
The above figures are reprinted by permission from Cell Press: Cell (1997, 91, 335-345) copyright 1997.
Secondary reference #1
Title
Author B.D.Guenther.
Ref. structural studies on the ...
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