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4mqv

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Crystal complex of Rpa32c and Smarcal1 N-terminus

Structural highlights

4mqv is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] 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.^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

Replication protein A subunit RPA32 contains a C-terminal domain that interacts with a variety of DNA damage response proteins including SMARCAL1, Tipin, UNG2 and XPA. We have solved the high-resolution crystal structure of RPA32 C-terminal domain (RPA32C) in complex with a 26-amino acid peptide derived from the N-terminus of SMARCAL1 (SMARCAL1N). The RPA32C-SMARCAL1N structure reveals a 1:1 binding stoichiometry and displays a well-ordered binding interface. SMARCAL1N adopts a long alpha-helical conformation with the highly conserved 11 residues aligned on one face of the alpha helix showing extensive interactions with the RPA32C domain. Extensive mutagenesis experiments were performed to corroborate the interactions observed in crystal structure. Moreover, the alpha1/alpha2 loop of RPA32C domain undergoes a conformational rearrangement upon SMARCAL1N binding. NMR study has further confirmed that the RPA32C-SMARCAL1N interaction induces the conformational changes in RPA32C. ITC studies have also demonstrated that the conserved alpha-helical motif defined in the current study is required for sufficient binding of RPA32C. Taken together, our study has provided convincing structural information that redefines the common recognition pattern shared by RPA32C interacting proteins. This article is protected by copyright. All rights reserved.

Structure of RPA32 bound to N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteins.,Xie S, Lu Y, Jakoncic J, Sun H, Xia J, Qian C FEBS J. 2014 Jun 9. doi: 10.1111/febs.12867. PMID:24910198^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Weisshart K, Pestryakov P, Smith RW, Hartmann H, Kremmer E, Lavrik O, Nasheuer HP. Coordinated regulation of replication protein A activities by its subunits p14 and p32. J Biol Chem. 2004 Aug 20;279(34):35368-76. Epub 2004 Jun 17. PMID:15205463 doi:10.1074/jbc.M403825200
↑ Mason AC, Haring SJ, Pryor JM, Staloch CA, Gan TF, Wold MS. An alternative form of replication protein a prevents viral replication in vitro. J Biol Chem. 2009 Feb 20;284(8):5324-31. doi: 10.1074/jbc.M808963200. Epub 2008, Dec 29. PMID:19116208 doi:10.1074/jbc.M808963200
↑ Kemp MG, Mason AC, Carreira A, Reardon JT, Haring SJ, Borgstahl GE, Kowalczykowski SC, Sancar A, Wold MS. An alternative form of replication protein a expressed in normal human tissues supports DNA repair. J Biol Chem. 2010 Feb 12;285(7):4788-97. doi: 10.1074/jbc.M109.079418. Epub 2009 , Dec 7. PMID:19996105 doi:10.1074/jbc.M109.079418
↑ Lee DH, Pan Y, Kanner S, Sung P, Borowiec JA, Chowdhury D. A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat Struct Mol Biol. 2010 Mar;17(3):365-72. doi: 10.1038/nsmb.1769. Epub 2010 Feb, 14. PMID:20154705 doi:10.1038/nsmb.1769
↑ Weisshart K, Pestryakov P, Smith RW, Hartmann H, Kremmer E, Lavrik O, Nasheuer HP. Coordinated regulation of replication protein A activities by its subunits p14 and p32. J Biol Chem. 2004 Aug 20;279(34):35368-76. Epub 2004 Jun 17. PMID:15205463 doi:10.1074/jbc.M403825200
↑ Mason AC, Haring SJ, Pryor JM, Staloch CA, Gan TF, Wold MS. An alternative form of replication protein a prevents viral replication in vitro. J Biol Chem. 2009 Feb 20;284(8):5324-31. doi: 10.1074/jbc.M808963200. Epub 2008, Dec 29. PMID:19116208 doi:10.1074/jbc.M808963200
↑ Kemp MG, Mason AC, Carreira A, Reardon JT, Haring SJ, Borgstahl GE, Kowalczykowski SC, Sancar A, Wold MS. An alternative form of replication protein a expressed in normal human tissues supports DNA repair. J Biol Chem. 2010 Feb 12;285(7):4788-97. doi: 10.1074/jbc.M109.079418. Epub 2009 , Dec 7. PMID:19996105 doi:10.1074/jbc.M109.079418
↑ Lee DH, Pan Y, Kanner S, Sung P, Borowiec JA, Chowdhury D. A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat Struct Mol Biol. 2010 Mar;17(3):365-72. doi: 10.1038/nsmb.1769. Epub 2010 Feb, 14. PMID:20154705 doi:10.1038/nsmb.1769
↑ Xie S, Lu Y, Jakoncic J, Sun H, Xia J, Qian C. Structure of RPA32 bound to N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteins. FEBS J. 2014 Jun 9. doi: 10.1111/febs.12867. PMID:24910198 doi:http://dx.doi.org/10.1111/febs.12867

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4mqv"

Categories: Homo sapiens | Large Structures | Qian CM | Xie S

@@ Line 3: / Line 3: @@
 <StructureSection load='4mqv' size='340' side='right'caption='[[4mqv]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4mqv]] is a 4 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=4MQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MQV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4mqv]] 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=4MQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MQV FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPA32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=4mqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mqv OCA], [https://pdbe.org/4mqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mqv RCSB], [https://www.ebi.ac.uk/pdbsum/4mqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mqv ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mqv OCA], [http://pdbe.org/4mqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mqv RCSB], [http://www.ebi.ac.uk/pdbsum/4mqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mqv ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/SMAL1_HUMAN SMAL1_HUMAN]] Schimke immuno-osseous dysplasia. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/SMAL1_HUMAN SMAL1_HUMAN]] ATP-dependent annealing helicase that catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA.<ref>PMID:18974355</ref>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Qian, C M]]
+[[Category: Qian CM]]
-[[Category: Xie, S]]
+[[Category: Xie S]]
-[[Category: Nucleus]]
-[[Category: Protein binding]]
-[[Category: Winged hth fold]]

4mqv

From Proteopedia

Current revision

Crystal complex of Rpa32c and Smarcal1 N-terminus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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