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New page: left|200px<br /> <applet load="1quq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1quq, resolution 2.5Å" /> '''COMPLEX OF REPLICATI...
 
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[[Image:1quq.gif|left|200px]]<br />
<applet load="1quq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1quq, resolution 2.5&Aring;" />
'''COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32'''<br />


==Overview==
==COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32==
Replication protein A (RPA), the eukaryote single-stranded DNA-binding, protein (SSB), is a heterotrimer. The largest subunit, RPA70, which, harbours the major DNA-binding activity, has two DNA-binding domains that, each adopt an OB-fold. The complex of the two smaller subunits, RPA32 and, RPA14, has weak DNA-binding activity but the mechanism of DNA binding is, unknown. We have determined the crystal structure of the proteolytic core, of RPA32 and RPA14, which consists of the central two-thirds of RPA32 and, the entire RPA14 subunit. The structure revealed that RPA14 and the, central part of RPA32 are structural homologues. Each subunit contains a, central OB-fold domain, which also resembles the DNA-binding domains in, RPA70; an N-terminal extension that interacts with the central OB-fold, domain; and a C-terminal helix that mediate heterodimerization via a, helix-helix interaction. The OB-fold of RPA32, but not RPA14, possesses, additional similarity to the RPA70 DNA-binding domains, supporting a, DNA-binding role for RPA32. The discovery of a third and fourth OB-fold in, RPA suggests that the quaternary structure of SSBs, which in Bacteria and, Archaea are also tetramers of OB-folds, is conserved in evolution. The, structure also suggests a mechanism for RPA trimer formation.
<StructureSection load='1quq' size='340' side='right'caption='[[1quq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1quq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUQ FirstGlance]. <br>
1QUQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1QUQ OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1quq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1quq OCA], [https://pdbe.org/1quq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1quq RCSB], [https://www.ebi.ac.uk/pdbsum/1quq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1quq ProSAT]</span></td></tr>
==Reference==
</table>
The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding., Bochkarev A, Bochkareva E, Frappier L, Edwards AM, EMBO J. 1999 Aug 16;18(16):4498-504. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10449415 10449415]
== Function ==
[https://www.uniprot.org/uniprot/RFA2_HUMAN RFA2_HUMAN] Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref>  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.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/1quq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1quq ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Bochkarev, A.]]
[[Category: Bochkarev A]]
[[Category: Bochkareva, E.]]
[[Category: Bochkareva E]]
[[Category: Edwards, A.M.]]
[[Category: Edwards AM]]
[[Category: Frappier, L.]]
[[Category: Frappier L]]
[[Category: ob-fold]]
[[Category: rpa]]
[[Category: ssdna-binding]]
 
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Retrieved from "https://proteopedia.org/1quq"