3LFO
Crystal structure of T. celer L30e E90A/R92A variant
Summary for 3LFO
| Entry DOI | 10.2210/pdb3lfo/pdb |
| Related | 1H7M |
| Descriptor | 50S ribosomal protein L30e (2 entities in total) |
| Functional Keywords | ribosomal protein, l30e, thermophilic, globular protein |
| Biological source | Thermococcus celer |
| Total number of polymer chains | 1 |
| Total formula weight | 10837.56 |
| Authors | Chan, C.H.,Wong, K.B. (deposition date: 2010-01-18, release date: 2010-04-14, Last modification date: 2023-11-01) |
| Primary citation | Chan, C.H.,Yu, T.H.,Wong, K.B. Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding. Plos One, 6:e21624-e21624, 2011 Cited by PubMed Abstract: Most thermophilic proteins tend to have more salt bridges, and achieve higher thermostability by up-shifting and broadening their protein stability curves. While the stabilizing effect of salt-bridge has been extensively studied, experimental data on how salt-bridge influences protein stability curves are scarce. Here, we used double mutant cycles to determine the temperature-dependency of the pair-wise interaction energy and the contribution of salt-bridges to ΔC(p) in a thermophilic ribosomal protein L30e. Our results showed that the pair-wise interaction energies for the salt-bridges E6/R92 and E62/K46 were stabilizing and insensitive to temperature changes from 298 to 348 K. On the other hand, the pair-wise interaction energies between the control long-range ion-pair of E90/R92 were negligible. The ΔC(p) of all single and double mutants were determined by Gibbs-Helmholtz and Kirchhoff analyses. We showed that the two stabilizing salt-bridges contributed to a reduction of ΔC(p) by 0.8-1.0 kJ mol⁻¹ K⁻¹. Taken together, our results suggest that the extra salt-bridges found in thermophilic proteins enhance the thermostability of proteins by reducing ΔC(p), leading to the up-shifting and broadening of the protein stability curves. PubMed: 21720566DOI: 10.1371/journal.pone.0021624 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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