PDBsum entry 5fox

Hydrolase

PDB id: 5fox

Contents

Protein chain

222 a.a.

Ligands

ACE-PHE-HIS-ALA-ALA-NH2

PO4

GOL

Waters ×299

PDB id:

5fox

Name:

Hydrolase

Title:

Humanised monomeric rada in complex with fhaa tetrapeptide

Structure:

DNA repair and recombination protein rada. Chain: a. Fragment: atpase, unp residues 108-349. Synonym: rada recombinase. Engineered: yes. Mutation: yes. Fhaa peptide. Chain: c. Engineered: yes.

Source:

Pyrococcus furiosus. Organism_taxid: 2261. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: pubs520. Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606

Resolution:

1.30Å R-factor: 0.158 R-free: 0.182

Authors:

D.E.Scott,M.Marsh,T.L.Blundell,C.Abell,M.Hyvonen

Key ref:

D.E.Scott et al. (2016). Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction. Febs Lett, 590, 1094-1102. PubMed id: 26992456 DOI: 10.1002/1873-3468.12139

Date:

26-Nov-15 Release date: 30-Mar-16

Protein chain

O74036  (RADA_PYRFU) -  DNA repair and recombination protein RadA from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Seq: 349 a.a.

Struc: 222 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.6.4.- - ?????

DOI no: 10.1002/1873-3468.12139

Febs Lett 590:1094-1102 (2016)

PubMed id: 26992456

Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction.

D.E.Scott, M.Marsh, T.L.Blundell, C.Abell, M.Hyvönen.

ABSTRACT

RAD51 is a recombinase involved in the homologous recombination of double-strand breaks in DNA. RAD51 forms oligomers by binding to another molecule of RAD51 via an 'FxxA' motif, and the same recognition sequence is similarly utilised to bind BRCA2. We have tabulated the effects of mutation of this sequence, across a variety of experimental methods and from relevant mutations observed in the clinic. We use mutants of a tetrapeptide sequence to probe the binding interaction, using both isothermal titration calorimetry and X-ray crystallography. Where possible, comparison between our tetrapeptide mutational study and the previously reported mutations is made, discrepancies are discussed and the importance of secondary structure in interpreting alanine scanning and mutational data of this nature is considered.