1SND
STAPHYLOCOCCAL NUCLEASE DIMER CONTAINING A DELETION OF RESIDUES 114-119 COMPLEXED WITH CALCIUM CHLORIDE AND THE COMPETITIVE INHIBITOR DEOXYTHYMIDINE-3',5'-DIPHOSPHATE
1SND の概要
エントリーDOI | 10.2210/pdb1snd/pdb |
分子名称 | STAPHYLOCOCCAL NUCLEASE DIMER (2 entities in total) |
機能のキーワード | hydrolase, nuclease, endonuclease |
由来する生物種 | Staphylococcus aureus |
細胞内の位置 | Nuclease A: Secreted. Nuclease B: Membrane: P00644 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 32253.04 |
構造登録者 | Green, S.M.,Gittis, A.G.,Meeker, A.K.,Lattman, E.E. (登録日: 1996-08-23, 公開日: 1997-04-21, 最終更新日: 2024-05-22) |
主引用文献 | Green, S.M.,Gittis, A.G.,Meeker, A.K.,Lattman, E.E. One-step evolution of a dimer from a monomeric protein. Nat.Struct.Biol., 2:746-751, 1995 Cited by PubMed Abstract: Deletion of six amino acids in a surface loop transforms staphylococcal nuclease from a monomeric protein into a very stable dimer (Kd < 1 x 10(-8)M). A 2 A X-ray crystal structure of the dimer (R = 0.176) shows that the carboxy-terminal alpha-helix has been stripped from its normal position in one monomer and is now incorporated into the equivalent position on the adjoining monomer. This swapping creates an association interface of 2900 A 2. A second, smaller interface of 460 A 2 is also formed. The spontaneous exchange or swapping of secondary structural elements provides a simple pathway for the formation of large, stable protein/protein interfaces and may play an important role in the evolution of oligomeric proteins. PubMed: 7552745DOI: 10.1038/nsb0995-746 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.84 Å) |
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