5JX4

Crystal structure of E36-G37del mutant of the Bacillus caldolyticus cold shock protein.

5JX4 の概要

• エントリーDOI: 10.2210/pdb5jx4/pdb
• 分子名称: Cold shock protein CspB, SULFATE ION (3 entities in total)
• 機能のキーワード: bccsp, monomer, mutant, cold shock protein., dna binding protein
• 由来する生物種: Bacillus caldolyticus
• 細胞内の位置: Cytoplasm: P41016
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15180.76

構造登録者

Carvajal, A.,Castro-Fernandez, V.,Cabrejos, D.,Fuentealba, M.,Pereira, H.M.,Vallejos, G.,Cabrera, R.,Garratt, R.C.,Komives, E.A.,Ramirez-Sarmiento, C.A.,Babul, J. (登録日: 2016-05-12, 公開日: 2017-05-10, 最終更新日: 2023-09-27)

主引用文献

Carvajal, A.I.,Vallejos, G.,Komives, E.A.,Castro-Fernandez, V.,Leonardo, D.A.,Garratt, R.C.,Ramirez-Sarmiento, C.A.,Babul, J.
Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.
FEBS J., 284:1882-1896, 2017

PubMed Abstract: Cold shock proteins (Csp) constitute a family of ubiquitous small proteins that act as RNA-chaperones to avoid cold-induced termination of translation. All members contain two subdomains composed of 2 and 3 β-strands, respectively, which are connected by a hinge loop and fold into a β-barrel. Bacillus caldolyticus Csp (BcCsp) is one of the most studied members of the family in terms of its folding, function, and structure. This protein has been described as a monomer in solution, although a recent crystal structure showed dimerization via domain swapping (DS). In contrast, other cold shock proteins of the same fold are known to dimerize in a nonswapped arrangement. Hypothesizing that reducing the size of the hinge loop may promote swapping as in several other DS proteins with different folds we deleted two residues from these region (BcCsp∆36-37), leading to a protein in monomer-dimer equilibrium with similar folding stability to that of the wild-type. Strikingly, the crystal structure of BcCsp∆36-37 revealed a nonswapped dimer with its interface located at the nucleic acid-binding surface, showing that the deletion led to structural consequences far from the perturbation site. Concomitantly, circular dichroism experiments on BcCsp∆36-37 demonstrated that binding of the oligonucleotide hexathymidine disrupts the dimer. Additionally, HDXMS shows a protective effect on the protein structure upon dimerization, where the resulting interactions between ligand-binding surfaces in the dimer reduced the extent of exchange throughout the whole protein. Our work provides evidence of the complex interplay between conformational dynamics, deletions, and oligomerization within the Csp protein family.

PubMed: 28457014
DOI: 10.1111/febs.14093

実験手法

X-RAY DIFFRACTION (1.8 Å)