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PDBsum entry 5fov
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PDB id:
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Hydrolase
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Title:
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Humanised monomeric rada in complex with fhtg tetrapeptide
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Structure:
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DNA repair and recombination protein rada. Chain: a, c. Fragment: atpase, unp residues 108-349. Engineered: yes. Mutation: yes. Fhtg peptide. Chain: e, f. Engineered: yes. Other_details: acetylated at the n-terminus and amidated in thE C-
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Source:
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Pyrococcus furiosus (strain atcc 43587 / dsm 3638 / jcm 8422 / vc1). Organism_taxid: 186497. Strain: atcc 43587 / dsm 3638 / jcm 8422 / vc1. Gene: rada, pf1926. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: pubs520. Synthetic: yes.
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Resolution:
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1.74Å
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R-factor:
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0.178
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R-free:
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0.216
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Authors:
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D.E.Scott,M.Marsh,T.L.Blundell,C.Abell,M.Hyvonen
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Key ref:
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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:
DOI:
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Date:
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26-Nov-15
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Release date:
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30-Mar-16
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PROCHECK
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Headers
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References
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O74036
(RADA_PYRFU) -
DNA repair and recombination protein RadA from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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Seq:
Struc:
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349 a.a.
227 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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DOI no:
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Febs Lett
590:1094-1102
(2016)
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PubMed id:
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Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction.
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D.E.Scott,
M.Marsh,
T.L.Blundell,
C.Abell,
M.Hyvönen.
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ABSTRACT
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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.
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Links
