PDBsum entry: 2k7f

Replication/DNA

PDB id: 2k7f

Contents

Protein chain

109 a.a. *

DNA/RNA

* Residue conservation analysis

PDB id:

2k7f

Name:

Replication/DNA

Title:

Haddock calculated model of the complex between the brct reg p140 and dsdna

Structure:

Replication factor c subunit 1. Chain: a. Fragment: brct domain (unp residues 375-480). Synonym: activator 1 subunit 1, replication factor c large rf-c 140 kda subunit, activator 1 140 kda subunit, a1 140 k subunit, activator 1 large subunit, DNA-binding protein po- engineered: yes. 5'-d(p Dcp Dgp Dap Dcp Dcp Dtp Dcp Dgp Dap Dgp Da da)-3'.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rfc1, rfc140. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic: yes

NMR struc:

4 models

Authors:

M.Kobayashi,E.Ab,A.Bonvin,G.Siegal

Key ref:

M.Kobayashi et al. (2010). 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, 285, 10087-10097. PubMed id: 20081198 DOI: 10.1074/jbc.M109.054106

Date:

10-Aug-08 Release date: 08-Sep-09

Protein chain

P35251  (RFC1_HUMAN) -  Replication factor C subunit 1

Seq: 1148 a.a.

Struc: 109 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: intracellular (1 term)

DOI no: 10.1074/jbc.M109.054106

J Biol Chem 285:10087-10097 (2010)

PubMed id: 20081198

Structure of the DNA-bound BRCA1 C-terminal region from human replication factor C p140 and model of the protein-DNA complex.

M.Kobayashi, E.Ab, A.M.Bonvin, G.Siegal.

ABSTRACT

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.