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1YF2

Three-dimensional structure of DNA sequence specificity (S) subunit of a type I restriction-modification enzyme and its functional implications

1YF2 の概要
エントリーDOI10.2210/pdb1yf2/pdb
分子名称Type I restriction-modification enzyme, S subunit (2 entities in total)
機能のキーワードtype i restriction modification enzyme, s-subunit, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, hydrolase regulator
由来する生物種Methanocaldococcus jannaschii
タンパク質・核酸の鎖数2
化学式量合計97279.11
構造登録者
Kim, J.S.,Degiovanni, A.,Jancarik, J.,Adams, P.D.,Yokota, H.A.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (登録日: 2004-12-30, 公開日: 2005-02-15, 最終更新日: 2024-02-14)
主引用文献Kim, J.S.,Degiovanni, A.,Jancarik, J.,Adams, P.D.,Yokota, H.,Kim, R.,Kim, S.H.
Crystal structure of DNA sequence specificity subunit of a type I restriction-modification enzyme and its functional implications.
Proc.Natl.Acad.Sci.USA, 102:3248-3253, 2005
Cited by
PubMed Abstract: Type I restriction-modification enzymes are differentiated from type II and type III enzymes by their recognition of two specific dsDNA sequences separated by a given spacer and cleaving DNA randomly away from the recognition sites. They are oligomeric proteins formed by three subunits: a specificity subunit, a methylation subunit, and a restriction subunit. We solved the crystal structure of a specificity subunit from Methanococcus jannaschii at 2.4-A resolution. Two highly conserved regions (CRs) in the middle and at the C terminus form a coiled-coil of long antiparallel alpha-helices. Two target recognition domains form globular structures with almost identical topologies and two separate DNA binding clefts with a modeled DNA helix axis positioned across the CR helices. The structure suggests that the coiled-coil CRs act as a molecular ruler for the separation between two recognized DNA sequences. Furthermore, the relative orientation of the two DNA binding clefts suggests kinking of bound dsDNA and exposing of target adenines from the recognized DNA sequences.
PubMed: 15728358
DOI: 10.1073/pnas.0409851102
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 1yf2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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