7P53
Crystal Structure of Human gamma-D-crystallin mutant C110M at 1.57 Angstroms resolution
Summary for 7P53
| Entry DOI | 10.2210/pdb7p53/pdb |
| Descriptor | Gamma-crystallin D (2 entities in total) |
| Functional Keywords | cysteine mutation, recombinant, structural protein, eye lens |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 20663.02 |
| Authors | Strofaldi, A.,Khan, A.R.,McManus, J. (deposition date: 2021-07-14, release date: 2021-10-13, Last modification date: 2024-01-31) |
| Primary citation | Strofaldi, A.,Khan, A.R.,McManus, J.J. Surface Exposed Free Cysteine Suppresses Crystallization of Human gamma D-Crystallin. J.Mol.Biol., 433:167252-167252, 2021 Cited by PubMed Abstract: Human γD-crystallin (HGD) has remarkable stability against condensation in the human lens, sometimes over a whole lifetime. The native protein has a surface exposed free cysteine that forms dimers (Benedek, 1997; Ramkumar et al., 1864) without specific biological function and leads to further protein association and/or aggregation, which creates a paradox for understanding its stability. Previous work has demonstrated that chemical modification of the protein at the free cysteine (C110), increases the temperature at which liquid-liquid phase separation occurs (LLPS), lowers protein solubility and suggests an important role for this amino acid in maintaining its long-term resistance to condensation. Here we demonstrate that mutation of the cysteine does not alter the structure or solubility (liquidus) line for the protein, but dramatically increases the protein crystal nucleation rate following LLPS, suggesting that the free cysteine has a vital role in suppressing crystallization in the human lens. PubMed: 34537240DOI: 10.1016/j.jmb.2021.167252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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