1a5t: Difference between revisions

Revision as of 16:11, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1a5t.png

Template:STRUCTURE 1a5t

CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE IIICRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III

Template:ABSTRACT PUBMED 9363942

About this StructureAbout this Structure

1A5T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III., Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J, Cell. 1997 Oct 31;91(3):335-45. PMID:9363942

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OCA

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+===CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9363942}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9363942}}
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 [[Category: Dna replication]]
 [[Category: Zinc finger]]
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