1l1o
From Proteopedia
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| - | [[Image:1l1o.gif|left|200px]] | + | [[Image:1l1o.gif|left|200px]] |
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| - | '''Structure of the human Replication Protein A (RPA) trimerization core''' | + | {{Structure |
| + | |PDB= 1l1o |SIZE=350|CAPTION= <scene name='initialview01'>1l1o</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |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]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of the human Replication Protein A (RPA) trimerization core''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L1O is a [ | + | 1L1O 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=1L1O OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11927569 11927569] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ssdna binding protein]] | [[Category: ssdna binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:25:07 2008'' |
Revision as of 10:25, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | |||||||
| Gene: | RFA3_HUMAN (Homo sapiens), RFA2_HUMAN (Homo sapiens), RFA1_HUMAN (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 12:25:07 2008
