1l1o

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[[Image:1l1o.gif|left|200px]]
[[Image:1l1o.gif|left|200px]]
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{{Structure
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|PDB= 1l1o |SIZE=350|CAPTION= <scene name='initialview01'>1l1o</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1l1o", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= RFA3_HUMAN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RFA2_HUMAN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RFA1_HUMAN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1l1o| PDB=1l1o | SCENE= }}
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|RELATEDENTRY=[[1jmc|1jmc]], [[1fgu|1fgu]], [[1quq|1quq]], [[1dpu|1dpu]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1o OCA], [http://www.ebi.ac.uk/pdbsum/1l1o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l1o RCSB]</span>
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'''Structure of the human Replication Protein A (RPA) trimerization core'''
'''Structure of the human Replication Protein A (RPA) trimerization core'''
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[[Category: Korolev, S.]]
[[Category: Korolev, S.]]
[[Category: Lees-Miller, S P.]]
[[Category: Lees-Miller, S P.]]
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[[Category: eukaryotic ssb]]
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[[Category: Eukaryotic ssb]]
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[[Category: ob-fold]]
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[[Category: Ob-fold]]
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[[Category: ssdna binding protein]]
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[[Category: Ssdna binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:26:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:44 2008''
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Revision as of 20:26, 2 May 2008

Image:1l1o.gif

Template:STRUCTURE 1l1o

Structure of the human Replication Protein A (RPA) trimerization core


Overview

The human single-stranded DNA-binding protein, replication protein A (RPA) binds DNA in at least two different modes: initial [8-10 nucleotides (nt)] and stable ( approximately 30 nt). Switching from 8 to 30 nt mode is associated with a large conformational change. Here we report the 2.8 A structure of the RPA trimerization core comprising the C-terminal DNA-binding domain of subunit RPA70 (DBD-C), the central DNA-binding domain of subunit RPA32 (DBD-D) and the entire RPA14 subunit. All three domains are built around a central oligonucleotide/oligosaccharide binding (OB)-fold and flanked by a helix at the C-terminus. Trimerization is mediated by three C-terminal helices arranged in parallel. The OB-fold of DBD-C possesses unique structural features; embedded zinc ribbon and helix-turn-helix motifs. Using time-resolved proteolysis with trypsin, we demonstrate that the trimerization core does not contribute to the binding with substrates of 10 nt, but interacts with oligonucleotides of 24 nt. Taken together, our data indicate that switching from 8-10 to 30 nt mode is mediated by DNA binding with the trimerization core.

About this Structure

1L1O is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA., Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A, EMBO J. 2002 Apr 2;21(7):1855-63. PMID:11927569 Page seeded by OCA on Fri May 2 23:26:25 2008

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