3Q37

Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using Two Triosephosphate Isomerases from Pathogenic Trypanosomes.

3Q37 の概要

• エントリーDOI: 10.2210/pdb3q37/pdb
• 関連するPDBエントリー: 1tcd 5tim
• 分子名称: TIM from Trypanosoma cruzi/ TIM from Trypanosoma brucei brucei chimera protein (2 entities in total)
• 機能のキーワード: tim barrel, isomerase
• 由来する生物種: Trypanosoma brucei brucei; 詳細
• 細胞内の位置: Glycosome: P52270
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 109288.98

構造登録者

Garcia-Torres, I.,Cabrera, N.,Torres-Larios, A.,Rodriguez-Bolanos, M.,Gomez-Puyou, A.,Perez-Montfort, R. (登録日: 2010-12-21, 公開日: 2011-09-14, 最終更新日: 2023-09-13)

主引用文献

Garcia-Torres, I.,Cabrera, N.,Torres-Larios, A.,Rodriguez-Bolanos, M.,Diaz-Mazariegos, S.,Gomez-Puyou, A.,Perez-Montfort, R.
Identification of amino acids that account for long-range interactions in two triosephosphate isomerases from pathogenic trypanosomes.
Plos One, 6:e18791-e18791, 2011

PubMed Abstract: For a better comprehension of the structure-function relationship in proteins it is necessary to identify the amino acids that are relevant for measurable protein functions. Because of the numerous contacts that amino acids establish within proteins and the cooperative nature of their interactions, it is difficult to achieve this goal. Thus, the study of protein-ligand interactions is usually focused on local environmental structural differences. Here, using a pair of triosephosphate isomerase enzymes with extremely high homology from two different organisms, we demonstrate that the control of a seventy-fold difference in reactivity of the interface cysteine is located in several amino acids from two structurally unrelated regions that do not contact the cysteine sensitive to the sulfhydryl reagent methylmethane sulfonate, nor the residues in its immediate vicinity. The change in reactivity is due to an increase in the apparent pKa of the interface cysteine produced by the mutated residues. Our work, which involved grafting systematically portions of one protein into the other protein, revealed unsuspected and multisite long-range interactions that modulate the properties of the interface cysteines and has general implications for future studies on protein structure-function relationships.

PubMed: 21533154
DOI: 10.1371/journal.pone.0018791

実験手法

X-RAY DIFFRACTION (1.65 Å)