1QUJ

PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH CHLORINE AND PHOSPHATE

1QUJ の概要

• エントリーDOI: 10.2210/pdb1quj/pdb
• 分子名称: PHOSPHATE-BINDING PROTEIN, CHLORIDE ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: binding protein, phosphate transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P06128
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34529.99

構造登録者

Yao, N.,Choudhary, A.,Ledvina, P.S.,Quiocho, F.A. (登録日: 1995-11-11, 公開日: 1996-07-11, 最終更新日: 2024-02-14)

主引用文献

Yao, N.,Ledvina, P.S.,Choudhary, A.,Quiocho, F.A.
Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor.
Biochemistry, 35:2079-2085, 1996

PubMed Abstract: Electrostatic interactions are among the key forces determining the structure and function of proteins. These are exemplified in the liganded form of the receptor, a phosphate binding protein from Escherichia coli. The phosphate, completely dehydrated and buried in the receptor, is bound by 12 hydrogen bonds as well as a salt link with Arg 135. We have modulated the ionic attraction while preserving the hydrogen bonds by mutating Asp 137, also salt linked to Arg 135, to Asn, Gly or Thr. High-resolution crystallographic analysis revealed that Gly and Thr (but not Asn) mutant proteins have incorporated a more electronegative Cl- in place of the Asp carboxylate. That no dramatic effect on phosphate affinity was produced by these ionic perturbations indicates a major role for hydrogen bonds and other local dipoles in the binding and charge stabilization of ionic ligands.

PubMed: 8652549
DOI: 10.1021/bi952686r

実験手法

X-RAY DIFFRACTION (1.9 Å)