Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus

Structure and interaction of Corynebacterium pseudotuberculosis cold shock protein A with Y‐box single‐stranded DNA fragment

“…The presence of a positively charged residue in the N‐terminal of Bc ‐CspB (R3) and Tm ‐Csp (R2) participating in an ion cluster is a characteristic of the thermophilic members of the Csp family; however, an alanine (A2) is found in the corresponding position in Cp ‐CspA. Therefore, the structural characteristics of the Cp ‐CspA and its T m match with the proposal in the literature which relates the thermal stability of Csps to their structural features, such as number of salt bridges, number of hydrophobic core residues, and charge balance on the protein surface .…”

“…), which are composed of clusters of residues located on the surface of the protein and contain predominantly hydrophobic, aromatic and basic residues. Structural alignment analysis shows that Cp ‐CspA has a backbone RMSD value of 0.727 Å with the crystal structure of St ‐CspE ; 0.772 and 1.925 Å with the crystal and NMR structure of Bs ‐CspB, respectively ; 0.684 and 0.716 Å with the crystal and NMR structure of Ec ‐CspA, respectively ; 0.805 Å with the crystal structure of Bc ‐CspB ; and 0.896 Å with the NMR structure of Ta ‐Csp (Fig. ).…”

“…Comparison of the Cp ‐CspA structure with other Csp structures. Superposition of the Cp ‐CspA (cyan) with other Csps: St ‐CspE [red, PDB ID : (crystal)] , Bs ‐CspB (green and blue, 1 CSP (crystal) and 1 NMF ( NMR ), respectively) , Ec ‐CspA (yellow and magenta, 1 MJC (crystal) and 2L15 ( NMR ), respectively) , Bc ‐CspB [orange, 1C9O (crystal)] , and Ta ‐Csp [light pink, 2MO0 ( NMR )] . The solvent‐exposed hydrophobic residue side chains are shown (W8, F15, F17, F28, Y31, and F39 for Cp ‐CspA).…”

“…The three‐dimensional structure of Cp ‐CspA adopts a β‐barrel fold consisting of five β‐strands, and the structure is similar to other Csp structures (Fig. ) []. Despite the primary and tertiary structures similarity of Csps from psychrophilic, mesophilic, thermophilic, and hyperthermophilic bacteria, these proteins exhibit significant differences in their T m of unfolding.…”

“…Despite the primary and tertiary structures similarity of Csps from psychrophilic, mesophilic, thermophilic, and hyperthermophilic bacteria, these proteins exhibit significant differences in their T m of unfolding. Studies have demonstrated that these different T m may rise from structural differences amongst Csps, including the number of salt bridges, number of hydrophobic core residues, and charge balance on the protein surface . The T m value for the denaturation process of Cp ‐CspA was ~ 54 ° C (Fig.…”