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The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers.
J Mol Biol. 2005 Feb 25; 346(3):919-31.JM

Abstract

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.

Authors+Show Affiliations

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

15713472

Citation

Sridharan, Sudharsan, et al. "The HPr Proteins From the Thermophile Bacillus Stearothermophilus Can Form Domain-swapped Dimers." Journal of Molecular Biology, vol. 346, no. 3, 2005, pp. 919-31.
Sridharan S, Razvi A, Scholtz JM, et al. The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers. J Mol Biol. 2005;346(3):919-31.
Sridharan, S., Razvi, A., Scholtz, J. M., & Sacchettini, J. C. (2005). The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers. Journal of Molecular Biology, 346(3), 919-31.
Sridharan S, et al. The HPr Proteins From the Thermophile Bacillus Stearothermophilus Can Form Domain-swapped Dimers. J Mol Biol. 2005 Feb 25;346(3):919-31. PubMed PMID: 15713472.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers. AU - Sridharan,Sudharsan, AU - Razvi,Abbas, AU - Scholtz,J Martin, AU - Sacchettini,James C, Y1 - 2004/12/23/ PY - 2004/10/07/received PY - 2004/12/02/revised PY - 2004/12/03/accepted PY - 2005/2/17/pubmed PY - 2005/3/19/medline PY - 2005/2/17/entrez SP - 919 EP - 31 JF - Journal of molecular biology JO - J Mol Biol VL - 346 IS - 3 N2 - 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. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/15713472/The_HPr_proteins_from_the_thermophile_Bacillus_stearothermophilus_can_form_domain_swapped_dimers_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(04)01578-5 DB - PRIME DP - Unbound Medicine ER -