1fgu

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(New page: 200px<br /> <applet load="1fgu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fgu, resolution 2.50&Aring;" /> '''SSDNA-BINDING DOMAI...)
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'''SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A'''<br />
'''SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A'''<br />
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==About this Structure==
==About this Structure==
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1FGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FGU OCA].
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1FGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGU OCA].
==Reference==
==Reference==
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[[Category: ssdna-binding protein]]
[[Category: ssdna-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:53:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:47:41 2008''

Revision as of 13:47, 15 February 2008


1fgu, resolution 2.50Å

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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

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