1EWQ

CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION

Summary for 1EWQ

• Entry DOI: 10.2210/pdb1ewq/pdb
• Descriptor: DNA (5'-D(*GP*CP*GP*AP*CP*GP*CP*TP*AP*GP*CP*GP*TP*GP*CP*GP*GP*CP*TP*CP*GP*TP*C)-3'), DNA (5'-D(*GP*GP*AP*CP*GP*AP*GP*CP*CP*GP*CP*CP*GP*CP*TP*AP*GP*CP*GP*TP*CP*G)-3'), DNA MISMATCH REPAIR PROTEIN MUTS, ... (6 entities in total)
• Functional Keywords: multiple domains of protein, mostly mixed alpha-beta structures, one domain is entirely helical, double stranded helix, replication-dna complex, replication/dna
• Biological source: Thermus aquaticus
• Total number of polymer chains: 4
• Total formula weight: 187444.87

Authors

Obmolova, G.,Ban, C.,Hsieh, P.,Yang, W. (deposition date: 2000-04-26, release date: 2000-10-23, Last modification date: 2024-11-20)

Primary citation

Obmolova, G.,Ban, C.,Hsieh, P.,Yang, W.
Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA.
Nature, 407:703-710, 2000

PubMed Abstract: DNA mismatch repair is critical for increasing replication fidelity in organisms ranging from bacteria to humans. MutS protein, a member of the ABC ATPase superfamily, recognizes mispaired and unpaired bases in duplex DNA and initiates mismatch repair. Mutations in human MutS genes cause a predisposition to hereditary nonpolyposis colorectal cancer as well as sporadic tumours. Here we report the crystal structures of a MutS protein and a complex of MutS with a heteroduplex DNA containing an unpaired base. The structures reveal the general architecture of members of the MutS family, an induced-fit mechanism of recognition between four domains of a MutS dimer and a heteroduplex kinked at the mismatch, a composite ATPase active site composed of residues from both MutS subunits, and a transmitter region connecting the mismatch-binding and ATPase domains. The crystal structures also provide a molecular framework for understanding hereditary nonpolyposis colorectal cancer mutations and for postulating testable roles of MutS.

PubMed: 11048710
DOI: 10.1038/35037509

Experimental method

X-RAY DIFFRACTION (2.2 Å)