1fgu: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A== | ==SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A== | ||
<StructureSection load='1fgu' size='340' side='right' caption='[[1fgu]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1fgu' size='340' side='right'caption='[[1fgu]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fgu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGU FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fgu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGU FirstGlance]. <br> | ||
| Line 28: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1fgu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1fgu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Single-stranded DNA-binding protein|Single-stranded DNA-binding protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 33: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Belegu, V]] | [[Category: Belegu, V]] | ||
[[Category: Bochkarev, A]] | [[Category: Bochkarev, A]] | ||
Revision as of 12:05, 23 October 2019
SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN ASSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A
Structural highlights
Function[RFA1_HUMAN] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.[1] [2] Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.[3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAlthough 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. 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||