Summary information and primary citation
- PDB-id
-
1fw6;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- replication-DNA
- Method
- X-ray (2.7 Å)
- Summary
- Crystal structure of a taq muts-DNA-adp ternary
complex
- Reference
-
Junop MS, Obmolova G, Rausch K, Hsieh P, Yang W (2001):
"Composite
active site of an ABC ATPase: MutS uses ATP to verify
mismatch recognition and authorize DNA repair."
Mol.Cell, 7, 1-12. doi:
10.1016/S1097-2765(01)00149-6.
- Abstract
- The MutS protein initiates DNA mismatch repair by
recognizing mispaired and unpaired bases embedded in duplex
DNA and activating endo- and exonucleases to remove the
mismatch. Members of the MutS family also possess a
conserved ATPase activity that belongs to the ATP binding
cassette (ABC) superfamily. Here we report the crystal
structure of a ternary complex of MutS-DNA-ADP and assays
of initiation of mismatch repair in conjunction with
perturbation of the composite ATPase active site by
mutagenesis. These studies indicate that MutS has to bind
both ATP and the mismatch DNA simultaneously in order to
activate the other mismatch repair proteins. We propose
that the MutS ATPase activity plays a proofreading role in
DNA mismatch repair, verification of mismatch recognition,
and authorization of repair.
