1QCV

RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON

1QCV の概要

• エントリーDOI: 10.2210/pdb1qcv/pdb
• 分子名称: PROTEIN (RUBREDOXIN VARIANT PFRD-XC4) (1 entity in total)
• 機能のキーワード: hyperthermophile, rubredoxin, electron transport
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5874.40

構造登録者

Strop, P.,Mayo, S.L. (登録日: 1999-05-10, 公開日: 2000-02-18, 最終更新日: 2024-05-01)

主引用文献

Strop, P.,Mayo, S.L.
Contribution of surface salt bridges to protein stability.
Biochemistry, 39:1251-1255, 2000

PubMed Abstract: The role of surface salt bridges in protein stabilization has been a source of controversy. Here we present the NMR structure of a hyperthermophilic rubredoxin variant (PFRD-XC4) and the thermodynamic analysis of two surface salt bridges by double mutant cycles. This analysis shows that the surface side chain to side chain salt bridge between Lys 6 and Glu 49 does not stabilize PFRD-XC4. The main chain to side chain salt bridge between the N-terminus and Glu 14 was, however, found to stabilize PFRD-XC4 by 1. 5 kcal mol(-)(1). The entropic cost of making a surface salt bridge involving the protein's backbone is reduced, since the backbone has already been immobilized upon protein folding.

PubMed: 10684603
DOI: 10.1021/bi992257j

実験手法

SOLUTION NMR