3THZ
Human MutSbeta complexed with an IDL of 6 bases (Loop6) and ADP
3THZ の概要
エントリーDOI | 10.2210/pdb3thz/pdb |
関連するPDBエントリー | 3THW 3THX 3THY |
分子名称 | DNA mismatch repair protein Msh2, DNA mismatch repair protein Msh3, DNA Loop6 minus strand, ... (5 entities in total) |
機能のキーワード | abc family atpase, mismatch recognition, mismatched unpaired idl dna, dna binding protein-dna complex, dna binding protein/dna |
由来する生物種 | Homo sapiens (human) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 225483.02 |
構造登録者 | |
主引用文献 | Gupta, S.,Gellert, M.,Yang, W. Mechanism of mismatch repair revealed by human MutS bound to unpaired DNA loops Nat.Struct.Mol.Biol., 19:72-78, 2012 Cited by PubMed Abstract: DNA mismatch repair corrects replication errors, thus reducing mutation rates and microsatellite instability. Genetic defects in this pathway cause Lynch syndrome and various cancers in humans. Binding of a mispaired or unpaired base by bacterial MutS and eukaryotic MutSα is well characterized. We report here crystal structures of human MutSβ in complex with DNA containing insertion-deletion loops (IDL) of two, three, four or six unpaired nucleotides. In contrast to eukaryotic MutSα and bacterial MutS, which bind the base of a mismatched nucleotide, MutSβ binds three phosphates in an IDL. DNA is severely bent at the IDL; unpaired bases are flipped out into the major groove and partially exposed to solvent. A normal downstream base pair can become unpaired; a single unpaired base can thereby be converted to an IDL of two nucleotides and recognized by MutSβ. The C-terminal dimerization domains form an integral part of the MutS structure and coordinate asymmetrical ATP hydrolysis by Msh2 and Msh3 with mismatch binding to signal for repair. PubMed: 22179786DOI: 10.1038/nsmb.2175 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (4.3 Å) |
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