1QCV

RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON

Summary for 1QCV

• Entry DOI: 10.2210/pdb1qcv/pdb
• Descriptor: PROTEIN (RUBREDOXIN VARIANT PFRD-XC4) (1 entity in total)
• Functional Keywords: hyperthermophile, rubredoxin, electron transport
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 5874.40

Authors

Strop, P.,Mayo, S.L. (deposition date: 1999-05-10, release date: 2000-02-18, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR