1DBP
IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS
1DBP の概要
| エントリーDOI | 10.2210/pdb1dbp/pdb |
| 分子名称 | D-RIBOSE-BINDING PROTEIN, beta-D-ribopyranose (3 entities in total) |
| 機能のキーワード | binding protein |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Periplasm : P02925 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 28715.59 |
| 構造登録者 | |
| 主引用文献 | Bjorkman, A.J.,Binnie, R.A.,Cole, L.B.,Zhang, H.,Hermodson, M.A.,Mowbray, S.L. Identical mutations at corresponding positions in two homologous proteins with nonidentical effects. J.Biol.Chem., 269:11196-11200, 1994 Cited by PubMed Abstract: The x-ray structure of a mutant (Gly72 to Asp) of the Escherichia coli ribose-binding protein with altered transport function has been solved and refined to 2.2-A resolution with a conventional R-factor (R-factor = [formula: see text]) of 16.0% and good stereochemistry. Comparison with the wild type ribose-binding protein shows that the structure is disturbed little at the actual mutation site, but quite appreciably in a neighboring loop. Changes in the surface of the protein at the site of mutation, however, seem to explain the functional effects. A corresponding mutation of the related glucose/galactose-binding protein has different structural and functional effects due to the different structural context of the mutation site in that protein. These results are consistent with the concept that these proteins have slightly different ways of interacting with the membrane components in transport and chemotaxis. PubMed: 8157648主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






