PDBsum entry 2mo0

DNA binding protein

PDB id: 2mo0

Contents

Protein chain

68 a.a.

PDB id:

2mo0

Name:

DNA binding protein

Title:

Backbone 1h, 13c, and 15n chemical shift assignments for cold shock protein, tacsp

Structure:

Cold-shock DNA-binding domain protein. Chain: a. Engineered: yes

Source:

Thermus aquaticus. Organism_taxid: 498848. Strain: y51mc23. Gene: taqdraft_4615. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

B.Jin,K.W.Jeong,Y.Kim

Key ref:

B.Jin et al. (2014). Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus. Biochem Biophys Res Commun, 451, 402-407. PubMed id: 25101648 DOI: 10.1016/j.bbrc.2014.07.127

Date:

17-Apr-14 Release date: 20-Aug-14

Protein chain

B7ABH3  (B7ABH3_THEAQ) -

DOI no: 10.1016/j.bbrc.2014.07.127

Biochem Biophys Res Commun 451:402-407 (2014)

PubMed id: 25101648

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

B.Jin, K.W.Jeong, Y.Kim.

ABSTRACT

The thermophilic bacterium Thermus aquaticus is a well-known source of Taq polymerase. Here, we studied the structure and dynamics of the T. aquaticus cold-shock protein (Ta-Csp) to better understand its thermostability using NMR spectroscopy. We found that Ta-Csp has a five-stranded β-barrel structure with five salt bridges which are important for more rigid structure and a higher melting temperature (76°C) of Ta-Csp compared to mesophilic and psychrophilic Csps. Microsecond to millisecond time scale exchange processes occur only at the β1-β2 surface region of the nucleic acid binding site with an average conformational exchange rate constant of 674s(-1). The results imply that thermophilic Ta-Csp has a more rigid structure and may not need high structural flexibility to accommodate nucleic acids upon cold shock compared to its mesophile and psychrophile counterparts.