1fgu: Difference between revisions

Revision as of 03:13, 1 July 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:1fgu.png

Template:STRUCTURE 1fgu

SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN ASSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A

Template:ABSTRACT PUBMED 11157767

About this StructureAbout this Structure

1FGU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding., Bochkareva E, Belegu V, Korolev S, Bochkarev A, EMBO J. 2001 Feb 1;20(3):612-8. PMID:11157767

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OCA

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-'''SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A'''
+===SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A===
-==Overview==
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-Although structures of single-stranded (ss)DNA-binding proteins (SSBs) have been reported with and without ssDNA, the mechanism of ssDNA binding in eukarya remains speculative. Here we report a 2.5 Angstroms structure of the ssDNA-binding domain of human replication protein A (RPA) (eukaryotic SSB), for which we previously reported a structure in complex with ssDNA. A comparison of free and bound forms of RPA revealed that ssDNA binding is associated with a major reorientation between, and significant conformational changes within, the structural modules--OB-folds--which comprise the DNA-binding domain. Two OB-folds, whose tandem orientation was stabilized by the presence of DNA, adopted multiple orientations in its absence. Within the OB-folds, extended loops implicated in DNA binding significantly changed conformation in the absence of DNA. Analysis of intermolecular contacts suggested the possibility that other RPA molecules and/or other proteins could compete with DNA for the same binding site. Using this mechanism, protein-protein interactions can regulate, and/or be regulated by DNA binding. Combined with available biochemical data, this structure also suggested a dynamic model for the DNA-binding mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_11157767}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11157767}}
 ==About this Structure==
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 [[Category: Ob-fold]]
 [[Category: Ssdna-binding protein]]
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