1DRK

PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE-BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS

1DRK の概要

• エントリーDOI: 10.2210/pdb1drk/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: 28659.53

構造登録者

Mowbray, S.L.,Bjorkman, A.J. (登録日: 1994-09-23, 公開日: 1995-01-26, 最終更新日: 2024-02-07)

主引用文献

Bjorkman, A.J.,Binnie, R.A.,Zhang, H.,Cole, L.B.,Hermodson, M.A.,Mowbray, S.L.
Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis.
J.Biol.Chem., 269:30206-30211, 1994

PubMed Abstract: A number of mutations at Gly134 of the periplasmic ribose-binding protein of Escherichia coli were examined by a combined biochemical and structural approach. Different mutations gave rise to different patterns of effects on the chemotaxis and transport functions. The smallest residue (alanine) had the least effect on transport, whereas large hydrophobic residues had the smallest effect on chemotaxis. Comparison of the x-ray crystal structure of the G134R mutant protein (2.5-A resolution) to that of the wild type (1.6-A resolution) showed that the basic structure of the protein was unaltered. The loss of chemotaxis and transport functions in this and similar mutant proteins must therefore be caused by relatively simple surface effects, which include a change in local main chain conformation. The loss of chemotaxis and transport functions resulting from the introduction of an alanine residue at position 134 was suppressed by an additional isoleucine to threonine mutation at residue 132. An x-ray structure of the I132T/G134A double mutant protein (2.2-A resolution) showed that the changes in local structure were accompanied by a diffuse pattern of structural changes in the surrounding region, implying that the suppression derives from a combination of sources.

PubMed: 7982928

実験手法

X-RAY DIFFRACTION (2 Å)