Summary for 5VH1
| Entry DOI | 10.2210/pdb5vh1/pdb |
| Descriptor | Gamma S-crystallin (2 entities in total) |
| Functional Keywords | crystallin lens beta sheet two domain, protein binding |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 20696.19 |
| Authors | Sagar, V.,Wistow, G. (deposition date: 2017-04-12, release date: 2017-05-24, Last modification date: 2023-10-04) |
| Primary citation | Sagar, V.,Chaturvedi, S.K.,Schuck, P.,Wistow, G. Crystal Structure of Chicken gamma S-Crystallin Reveals Lattice Contacts with Implications for Function in the Lens and the Evolution of the beta gamma-Crystallins. Structure, 25:1068-1078.e2, 2017 Cited by PubMed Abstract: Previous attempts to crystallize mammalian γS-crystallin were unsuccessful. Native L16 chicken γS crystallized avidly while the Q16 mutant did not. The X-ray structure for chicken γS at 2.3 Å resolution shows the canonical structure of the superfamily plus a well-ordered N arm aligned with a β sheet of a neighboring N domain. L16 is also in a lattice contact, partially shielded from solvent. Unexpectedly, the major lattice contact matches a conserved interface (QR) in the multimeric β-crystallins. QR shows little conservation of residue contacts, except for one between symmetry-related tyrosines, but molecular dipoles for the proteins with QR show striking similarities while other γ-crystallins differ. In γS, QR has few hydrophobic contacts and features a thin layer of tightly bound water. The free energy of QR is slightly repulsive and analytical ultracentrifugation confirms no dimerization in solution. The lattice contacts suggest how γ-crystallins allow close packing without aggregation in the crowded environment of the lens. PubMed: 28648607DOI: 10.1016/j.str.2017.05.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
