1Y50

X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein (Hpr) F29W mutant domain_swapped dimer

1Y50 の概要

• エントリーDOI: 10.2210/pdb1y50/pdb
• 関連するPDBエントリー: 1Y4Y
• 分子名称: Phosphocarrier protein HPr, SULFATE ION (3 entities in total)
• 機能のキーワード: bacillus stearothermophilus f29w mutant domain-swapped dimer, transport protein
• 由来する生物種: Geobacillus stearothermophilus
• 細胞内の位置: Cytoplasm: P42013
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9503.79

構造登録者

Sridharan, S.,Razvi, A.,Scholtz, J.M.,Sacchettini, J.C. (登録日: 2004-12-01, 公開日: 2005-02-22, 最終更新日: 2024-04-03)

主引用文献

Sridharan, S.,Razvi, A.,Scholtz, J.M.,Sacchettini, J.C.
The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers.
J.Mol.Biol., 346:919-931, 2005

PubMed 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.

PubMed: 15713472
DOI: 10.1016/j.jmb.2004.12.008

実験手法

X-RAY DIFFRACTION (2 Å)