2MO1
Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7
Summary for 2MO1
| Entry DOI | 10.2210/pdb2mo1/pdb |
| Related | 2MO0 |
| NMR Information | BMRB: 19916 |
| Descriptor | Cold-shock DNA-binding domain protein (1 entity in total) |
| Functional Keywords | cold shock protein, thermus aquaticus, protein stability, protein binding, dna binding protein |
| Biological source | Thermus aquaticus |
| Cellular location | Cytoplasm (By similarity): B7ABH3 |
| Total number of polymer chains | 1 |
| Total formula weight | 7692.65 |
| Authors | Jin, B.,Jeong, K.W.,Kim, Y. (deposition date: 2014-04-17, release date: 2014-08-20, Last modification date: 2024-05-15) |
| Primary citation | Jin, B.,Jeong, K.W.,Kim, Y. Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus. Biochem.Biophys.Res.Commun., 451:402-407, 2014 Cited by PubMed 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 674 s(-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. PubMed: 25101648DOI: 10.1016/j.bbrc.2014.07.127 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
