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1DBP

IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS

1DBP の概要
エントリーDOI10.2210/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
Mowbray, S.L.,Joakim Bjorkman, A.J. (登録日: 1994-01-31, 公開日: 1994-05-31, 最終更新日: 2024-02-07)
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
Validation report summary of 1dbp
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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