5VH1

Crystal Structure of Chicken Gamma S Crystallin

「5V14」から置き換えられました

5VH1 の概要

• エントリーDOI: 10.2210/pdb5vh1/pdb
• 分子名称: Gamma S-crystallin (2 entities in total)
• 機能のキーワード: crystallin lens beta sheet two domain, protein binding
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20696.19

構造登録者

Sagar, V.,Wistow, G. (登録日: 2017-04-12, 公開日: 2017-05-24, 最終更新日: 2023-10-04)

主引用文献

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

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: 28648607
DOI: 10.1016/j.str.2017.05.015

実験手法

X-RAY DIFFRACTION (2.3 Å)