7ZVM
Thermococcus barophilus phosphomannose isomerase protein structure at 1.6 A
Summary for 7ZVM
| Entry DOI | 10.2210/pdb7zvm/pdb |
| Descriptor | Mannose-6-phosphate isomerase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | high pressure, protein dynamics, neutron scaterring, isomerase |
| Biological source | Thermococcus barophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 13409.68 |
| Authors | |
| Primary citation | Calio, A.,Dubois, C.,Fontanay, S.,Koza, M.M.,Hoh, F.,Roumestand, C.,Oger, P.,Peters, J. Unravelling the Adaptation Mechanisms to High Pressure in Proteins. Int J Mol Sci, 23:-, 2022 Cited by PubMed Abstract: Life is thought to have appeared in the depth of the sea under high hydrostatic pressure. Nowadays, it is known that the deep biosphere hosts a myriad of life forms thriving under high-pressure conditions. However, the evolutionary mechanisms leading to their adaptation are still not known. Here, we show the molecular bases of these mechanisms through a joint structural and dynamical study of two orthologous proteins. We observed that pressure adaptation involves the decoupling of protein-water dynamics and the elimination of cavities in the protein core. This is achieved by rearranging the charged residues on the protein surface and using bulkier hydrophobic residues in the core. These findings will be the starting point in the search for a complete genomic model explaining high-pressure adaptation. PubMed: 35955607DOI: 10.3390/ijms23158469 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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