1y51
From Proteopedia
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X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein (Hpr) F29W mutant
Overview
The study of proteins from extremophilic organisms continues to generate, interest in the field of protein folding because paradigms explaining the, enhanced stability of these proteins still elude us and such studies have, the potential to further our knowledge of the forces stabilizing proteins., We have undertaken such a study with our model protein HPr from a, mesophile, Bacillus subtilis, and a thermophile, Bacillus, stearothermophilus. We report here the high-resolution structures of the, wild-type HPr protein from the thermophile and a variant, F29W. The, variant proved to crystallize in two forms: a monomeric form with a, structure very similar to the wild-type protein as well as a, domain-swapped dimer. Interestingly, the structure of the domain-swapped, dimer for HPr is very different from that observed for a homologous, protein, Crh, from B.subtilis. The existence of a domain-swapped dimer has, implications for amyloid formation and is consistent with recent results, showing that the HPr proteins can form amyloid fibrils. We also, characterized the conformational stability of the thermophilic HPr, proteins using thermal and solvent denaturation methods and have used the, high-resolution structures in an attempt to explain the differences in, stability between the different HPr proteins. Finally, we present a, detailed analysis of the solution properties of the HPr proteins using a, variety of biochemical and biophysical methods.
About this Structure
1Y51 is a Single protein structure of sequence from Geobacillus stearothermophilus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers., Sridharan S, Razvi A, Scholtz JM, Sacchettini JC, J Mol Biol. 2005 Feb 25;346(3):919-31. Epub 2004 Dec 23. PMID:15713472
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