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1fgu

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[[Image:1fgu.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgu OCA], [http://www.ebi.ac.uk/pdbsum/1fgu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fgu RCSB]</span>
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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'''
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[[Category: Bochkareva, E.]]
[[Category: Bochkareva, E.]]
[[Category: Korolev, S.]]
[[Category: Korolev, S.]]
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[[Category: ob-fold]]
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[[Category: Ob-fold]]
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[[Category: ssdna-binding protein]]
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[[Category: Ssdna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:18:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:22:39 2008''
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Revision as of 13:18, 2 May 2008

Template:STRUCTURE 1fgu

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


Overview

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.

About this Structure

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

Reference

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 Page seeded by OCA on Fri May 2 16:18:38 2008

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