1D02
CRYSTAL STRUCTURE OF MUNI RESTRICTION ENDONUCLEASE IN COMPLEX WITH COGNATE DNA
1D02 の概要
| エントリーDOI | 10.2210/pdb1d02/pdb |
| 分子名称 | DNA (5'-D(*GP*CP*CP*AP*AP*TP*TP*GP*GP*C)-3'), TYPE II RESTRICTION ENZYME MUNI (3 entities in total) |
| 機能のキーワード | alpha/beta protein, protein-dna complex, distorted double helix, hydrolase-dna complex, hydrolase/dna |
| 由来する生物種 | Mycoplasma 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 52842.91 |
| 構造登録者 | Deibert, M.,Grazulis, S.,Janulaitis, A.,Siksnys, V.,Huber, R. (登録日: 1999-09-08, 公開日: 2000-03-08, 最終更新日: 2024-02-07) |
| 主引用文献 | Deibert, M.,Grazulis, S.,Janulaitis, A.,Siksnys, V.,Huber, R. Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 A resolution. EMBO J., 18:5805-5816, 1999 Cited by PubMed Abstract: The MunI restriction enzyme recognizes the palindromic hexanucleotide sequence C/AATTG (the '/' indicates the cleavage site). The crystal structure of its active site mutant D83A bound to cognate DNA has been determined at 1.7 A resolution. Base-specific contacts between MunI and DNA occur exclusively in the major groove. While DNA-binding sites of most other restriction enzymes are comprised of discontinuous sequence segments, MunI combines all residues involved in the base-specific contacts within one short stretch (residues R115-R121) located at the N-terminal region of the 3(10)4 helix. The outer CG base pair of the recognition sequence is recognized solely by R115 through hydrogen bonds made by backbone and side chain atoms to both bases. The mechanism of recognition of the central AATT nucleotides by MunI is similar to that of EcoRI, which recognizes the G/AATTC sequence. The local conformation of AATT deviates from the typical B-DNA form and is remarkably similar to EcoRI-DNA. It appears to be essential for specific hydrogen bonding and recognition by MunI and EcoRI. PubMed: 10545092DOI: 10.1093/emboj/18.21.5805 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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