2k7f

From Proteopedia

(Difference between revisions)

Revision as of 19:25, 24 December 2014

HADDOCK calculated model of the complex between the BRCT region of RFC p140 and dsDNA

Structural highlights

2k7f is a 3 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2k6g, 2ebu
Gene:	RFC1, RFC140 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[RFC1_HUMAN] The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.^[1] Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.^[2]

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 PubMed

BRCA1 C-terminal domain (BRCT)-containing proteins are found widely throughout the animal and bacteria kingdoms where they are exclusively involved in cell cycle regulation and DNA metabolism. Whereas most BRCT domains are involved in protein-protein interactions, a small subset has bona fide DNA binding activity. Here, we present the solution structure of the BRCT region of the large subunit of replication factor C bound to DNA and a model of the structure-specific complex with 5'-phosphorylated double-stranded DNA. The replication factor C BRCT domain possesses a large basic patch on one face, which includes residues that are structurally conserved and ligate the phosphate in phosphopeptide binding BRCT domains. An extra alpha-helix at the N terminus, which is required for DNA binding, inserts into the major groove and makes extensive contacts to the DNA backbone. The model of the protein-DNA complex suggests 5'-phosphate recognition by the BRCT domains of bacterial NAD(+)-dependent ligases and a nonclamp loading role for the replication factor C complex in DNA transactions.

Structure of the DNA-bound BRCA1 C-terminal region from human replication factor C p140 and model of the protein-DNA complex.,Kobayashi M, Ab E, Bonvin AM, Siegal G J Biol Chem. 2010 Mar 26;285(13):10087-97. Epub 2010 Jan 15. PMID:20081198^[3]

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

References

↑ Mossi R, Jonsson ZO, Allen BL, Hardin SH, Hubscher U. Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J Biol Chem. 1997 Jan 17;272(3):1769-76. PMID:8999859
↑ Mossi R, Jonsson ZO, Allen BL, Hardin SH, Hubscher U. Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J Biol Chem. 1997 Jan 17;272(3):1769-76. PMID:8999859
↑ Kobayashi M, Ab E, Bonvin AM, Siegal G. Structure of the DNA-bound BRCA1 C-terminal region from human replication factor C p140 and model of the protein-DNA complex. J Biol Chem. 2010 Mar 26;285(13):10087-97. Epub 2010 Jan 15. PMID:20081198 doi:10.1074/jbc.M109.054106

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k7f"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2k7f]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K7F FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k6g|2k6g]], [[2ebu|2ebu]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k6g|2k6g]], [[2ebu|2ebu]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RFC1, RFC140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RFC1, RFC140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k7f RCSB], [http://www.ebi.ac.uk/pdbsum/2k7f PDBsum]</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=2k7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k7f RCSB], [http://www.ebi.ac.uk/pdbsum/2k7f PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RFC1_HUMAN RFC1_HUMAN]] The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.<ref>PMID:8999859</ref>   Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.<ref>PMID:8999859</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Ab, E.]]
+[[Category: Ab, E]]
-[[Category: Bonvin, A.]]
+[[Category: Bonvin, A]]
-[[Category: Kobayashi, M.]]
+[[Category: Kobayashi, M]]
-[[Category: Siegal, G.]]
+[[Category: Siegal, G]]
 [[Category: Activator]]
 [[Category: Atp-binding]]

2k7f

From Proteopedia

Revision as of 19:25, 24 December 2014

HADDOCK calculated model of the complex between the BRCT region of RFC p140 and dsDNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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