6I5F

Crystal structure of DNA-free E.coli MutS P839E dimer mutant

6I5F の概要

• エントリーDOI: 10.2210/pdb6i5f/pdb
• 分子名称: DNA mismatch repair protein MutS, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: muts, dna mismatch repair, helix folding, abc-atpase, coiled coil, helix kink, apo-muts, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 193691.77

構造登録者

Bhairosing-Kok, D.,Groothuizen, F.S.,Fish, A.,Dharadhar, S.,Winterwerp, H.H.K.,Sixma, T.K. (登録日: 2018-11-13, 公開日: 2019-08-14, 最終更新日: 2024-01-24)

主引用文献

Bhairosing-Kok, D.,Groothuizen, F.S.,Fish, A.,Dharadhar, S.,Winterwerp, H.H.K.,Sixma, T.K.
Sharp kinking of a coiled-coil in MutS allows DNA binding and release.
Nucleic Acids Res., 47:8888-8898, 2019

PubMed Abstract: DNA mismatch repair (MMR) corrects mismatches, small insertions and deletions in DNA during DNA replication. While scanning for mismatches, dimers of MutS embrace the DNA helix with their lever and clamp domains. Previous studies indicated generic flexibility of the lever and clamp domains of MutS prior to DNA binding, but whether this was important for MutS function was unknown. Here, we present a novel crystal structure of DNA-free Escherichia coli MutS. In this apo-structure, the clamp domains are repositioned due to kinking at specific sites in the coiled-coil region in the lever domains, suggesting a defined hinge point. We made mutations at the coiled-coil hinge point. The mutants made to disrupt the helical fold at the kink site diminish DNA binding, whereas those made to increase stability of coiled-coil result in stronger DNA binding. These data suggest that the site-specific kinking of the coiled-coil in the lever domain is important for loading of this ABC-ATPase on DNA.

PubMed: 31372631
DOI: 10.1093/nar/gkz649

実験手法

X-RAY DIFFRACTION (2.6 Å)