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 Cited by 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: 10684603DOI: 10.1021/bi992257j PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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