1JY5
RNase-related protein from Calystegia sepium
1JY5 の概要
エントリーDOI | 10.2210/pdb1jy5/pdb |
分子名称 | CalsepRRP (2 entities in total) |
機能のキーワード | rnase, alpha-beta protein, hydrolase |
由来する生物種 | Calystegia sepium (hedge bindweed) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 46798.30 |
構造登録者 | Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.M.,Peumans, W.J.,De Ranter, C.J. (登録日: 2001-09-11, 公開日: 2002-04-10, 最終更新日: 2023-10-25) |
主引用文献 | Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.,Peumans, W.J.,De Ranter, C.J. Structure of an RNase-related protein from Calystegia sepium. Acta Crystallogr.,Sect.D, 58:627-633, 2002 Cited by PubMed Abstract: The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical alpha + beta structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the 'active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity. PubMed: 11914487DOI: 10.1107/S090744490200255X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.05 Å) |
構造検証レポート
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