Cold Shock Protein A from Corynebacterium pseudotuberculosis: Role of Electrostatic Forces in the Stability of the Secondary Structure.
The conformational stability of the Cold shock protein A (CspA) from C. pseudotuberculosis (Cp), a nucleic acid binding protein in function of pH and salt concentration was examined by using differential scanning calorimetry and CD spectroscopy in combination with computational analysis to identify the specify amino acids undergoing change. Our approach identified a sodiumbinding site in CpCspA and at pH 8.0 a significant reduction in the β-sheet content was observed which resulted in a decrease of the protein thermal stability. The computational analyses identified His30 and His65 as the amino acids with the largest charge shifts at different pHs. His30/His65 are part of the extensive hydrogen bonding network and along with the ion-binding site are essential for the conformational stability of CspA.
Multiuser Center for Biomolecular Innovation, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Monika A
MA
Coronado
Department of Physics, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Icaro P
IP
Caruso
Department of Physics, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Vinicius M de
VM
Oliveira
Department of Physics, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Vinícius G
VG
Contessoto
Department of Physics, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Vitor B P
VBP
Leite
Multiuser Center for Biomolecular Innovation, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Liege A
LA
Kawai
Multiuser Center for Biomolecular Innovation, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Raghuvir K
RK
Arni
Multiuser Center for Biomolecular Innovation, Universidade Estadual Paulista (UNESP), Rua Cristovao Colombo 2265, Sao Jose do Rio Preto-SP, 15054-000. Brazil.
Raphael J
RJ
Eberle
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D016925:Corynebacterium pseudotuberculosis / Q000737:chemistry* / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D011485:Protein Binding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012964:Sodium / Q000737:chemistry / Q000378:metabolism; D055672:Static Electricity
D001426:Bacterial Proteins; D011994:Recombinant Proteins; C062260:cold shock protein CS7.4, Bacteria; D006859:Hydrogen; D012964:Sodium
C. pseudotuberculosis; Cold shock protein; histidine; ion binding; pH; secondary structure