1E8J

SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS ZINC RUBREDOXIN, NMR, 20 STRUCTURES

Summary for 1E8J

• Entry DOI: 10.2210/pdb1e8j/pdb
• Descriptor: RUBREDOXIN (1 entity in total)
• Functional Keywords: electron transport, zinc-substitution, thermostability
• Biological source: DESULFOVIBRIO GIGAS
• Total number of polymer chains: 1
• Total formula weight: 5682.30

Authors

Lamosa, P.,Brennan, L.,Vis, H.,Turner, D.L.,Santos, H. (deposition date: 2000-09-21, release date: 2001-10-18, Last modification date: 2024-05-15)

Primary citation

Lamosa, P.,Brennan, L.,Vis, H.,Turner, D.L.,Santos, H.
NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes.
Extremophiles, 5:303-311, 2001

PubMed Abstract: Rubredoxins are small, soluble proteins that display a wide variation in thermostability, despite having a high degree of sequence similarity They also vary in the extent to which they are stabilized by solutes such as diglycerol phosphate. Hence, they provide excellent models for studying the mechanisms of thermostabilization. Nuclear magnetic resonance (NMR) spectroscopy can be used to investigate interactions between molecules, as well as subtle changes in conformation in solution, and also provides a means to measure protein stability. The assignment of the proton NMR spectrum of the zinc rubredoxin from Desulfovibrio gigas is presented, together with its structure in solution. The stabilizing effect of diglycerol phosphate on rubredoxin is demonstrated and assessed by determining selected amide proton exchange rates; diglycerol phosphate at 100 mM concentration caused an additional structural stabilization of 1.2 +/-0.4 kJ/mol. The pattern of effects on the exchange rates is discussed in relation to the protein structure.

PubMed: 11699644

Experimental method

SOLUTION NMR