3ZLJ

CRYSTAL STRUCTURE OF FULL-LENGTH E.COLI DNA MISMATCH REPAIR PROTEIN MUTS D835R MUTANT IN COMPLEX WITH GT MISMATCHED DNA

3ZLJ の概要

• エントリーDOI: 10.2210/pdb3zlj/pdb
• 分子名称: DNA MISMATCH REPAIR PROTEIN MUTS, 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP *AP*GP*TP*GP*TP*CP*AP)-3', 5'-D(*TP*GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP *GP*GP*CP*AP*GP*CP*TP)-3', ... (4 entities in total)
• 機能のキーワード: dna binding protein-dna complex, dimer mutant, mismatch repair, dna repair protein, dna damage, nucleotide-binding, atp-binding, dna binding protein/dna
• 由来する生物種: ESCHERICHIA COLI K-12; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 203735.11

構造登録者

Groothuizen, F.S.,Fish, A.,Petoukhov, M.V.,Reumer, A.,Manelyte, L.,Winterwerp, H.H.K.,Marinus, M.G.,Lebbink, J.H.G.,Svergun, D.I.,Friedhoff, P.,Sixma, T.K. (登録日: 2013-02-01, 公開日: 2013-07-17, 最終更新日: 2023-12-20)

主引用文献

Groothuizen, F.S.,Fish, A.,Petoukhov, M.V.,Reumer, A.,Manelyte, L.,Winterwerp, H.H.K.,Marinus, M.G.,Lebbink, J.H.G.,Svergun, D.I.,Friedhoff, P.,Sixma, T.K.
Using Stable Muts Dimers and Tetramers to Quantitatively Analyze DNA Mismatch Recognition and Sliding Clamp Formation.
Nucleic Acids Res., 41:8166-, 2013

PubMed Abstract: The process of DNA mismatch repair is initiated when MutS recognizes mismatched DNA bases and starts the repair cascade. The Escherichia coli MutS protein exists in an equilibrium between dimers and tetramers, which has compromised biophysical analysis. To uncouple these states, we have generated stable dimers and tetramers, respectively. These proteins allowed kinetic analysis of DNA recognition and structural analysis of the full-length protein by X-ray crystallography and small angle X-ray scattering. Our structural data reveal that the tetramerization domains are flexible with respect to the body of the protein, resulting in mostly extended structures. Tetrameric MutS has a slow dissociation from DNA, which can be due to occasional bending over and binding DNA in its two binding sites. In contrast, the dimer dissociation is faster, primarily dependent on a combination of the type of mismatch and the flanking sequence. In the presence of ATP, we could distinguish two kinetic groups: DNA sequences where MutS forms sliding clamps and those where sliding clamps are not formed efficiently. Interestingly, this inability to undergo a conformational change rather than mismatch affinity is correlated with mismatch repair.

PubMed: 23821665
DOI: 10.1093/NAR/GKT582

実験手法

X-RAY DIFFRACTION (3.1 Å)