2OK2

MutS C-terminal domain fused to Maltose Binding Protein

Summary for 2OK2

• Entry DOI: 10.2210/pdb2ok2/pdb
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein, DNA mismatch repair protein mutS fusion protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: dna repair, mismatch repair, tetramerization, sugar binding protein
• Biological source: Escherichia coli K12; More
• Total number of polymer chains: 2
• Total formula weight: 89567.01

Authors

Putnam, C.D.,Mendillo, M.L.,Kolodner, R.D. (deposition date: 2007-01-15, release date: 2007-04-10, Last modification date: 2023-08-30)

Primary citation

Mendillo, M.L.,Putnam, C.D.,Kolodner, R.D.
Escherichia coli MutS Tetramerization Domain Structure Reveals That Stable Dimers but Not Tetramers Are Essential for DNA Mismatch Repair in Vivo.
J.Biol.Chem., 282:16345-16354, 2007

PubMed Abstract: The Escherichia coli mispair-binding protein MutS forms dimers and tetramers in vitro, although the functional form in vivo is under debate. Here we demonstrate that the MutS tetramer is extended in solution using small angle x-ray scattering and the crystal structure of the C-terminal 34 amino acids of MutS containing the tetramer-forming domain fused to maltose-binding protein (MBP). Wild-type C-terminal MBP fusions formed tetramers and could bind MutS and MutS-MutL-DNA complexes. In contrast, D835R and R840E mutations predicted to disrupt tetrameric interactions only allowed dimerization of MBP. A chromosomal MutS truncation mutation eliminating the dimerization/tetramerization domain eliminated mismatch repair, whereas the tetramer-disrupting MutS D835R and R840E mutations only modestly affected MutS function. These results demonstrate that dimerization but not tetramerization of the MutS C terminus is essential for mismatch repair.

PubMed: 17426027
DOI: 10.1074/jbc.M700858200

Experimental method

X-RAY DIFFRACTION (2 Å)