1quq

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[[Image:1quq.gif|left|200px]]
 
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{{Structure
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==COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32==
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|PDB= 1quq |SIZE=350|CAPTION= <scene name='initialview01'>1quq</scene>, resolution 2.5&Aring;
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<StructureSection load='1quq' size='340' side='right'caption='[[1quq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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>
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|GENE=
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1quq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1quq OCA], [http://www.ebi.ac.uk/pdbsum/1quq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1quq RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/1quq_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</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].
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1QUQ is a [[Protein complex]] structure of sequences 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=1QUQ OCA].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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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://www.ncbi.nlm.nih.gov/pubmed/10449415 10449415]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bochkarev, A.]]
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[[Category: Bochkarev A]]
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[[Category: Bochkareva, E.]]
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[[Category: Bochkareva E]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards AM]]
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[[Category: Frappier, L.]]
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[[Category: Frappier L]]
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[[Category: ob-fold]]
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[[Category: rpa]]
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[[Category: ssdna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:16 2008''
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Current revision

COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32

PDB ID 1quq

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