1ZWM

NMR structure of murine gamma-S crystallin

1ZWM の概要

• エントリーDOI: 10.2210/pdb1zwm/pdb
• 関連するPDBエントリー: 1A45 1A5D 1A7H 1AG4 1AMM 1HK0 1ZWO
• 分子名称: Gamma crystallin S (1 entity in total)
• 機能のキーワード: alignment, deuteration, liquid crystal, pf1, relaxation, rdc, residual dipolar coupling, molecular fragment replacement, mfr, structural protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20747.27

構造登録者

Wu, Z.,Delaglio, F.,Wyatt, K.,Wistow, G.,Bax, A. (登録日: 2005-06-03, 公開日: 2005-07-05, 最終更新日: 2024-05-22)

主引用文献

Wu, Z.,Delaglio, F.,Wyatt, K.,Wistow, G.,Bax, A.
Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.
Protein Sci., 14:3101-3114, 2005

PubMed Abstract: The solution structure of murine gammaS-crystallin (gammaS) has been determined by multidimensional triple resonance NMR spectroscopy, using restraints derived from two sets of dipolar couplings, recorded in different alignment media, and supplemented by a small number of NOE distance restraints. gammaS consists of two topologically similar domains, arranged with an approximate twofold symmetry, and each domain shows close structural homology to closely related (approximately 50% sequence identity) domains found in other members of the gamma-crystallin family. Each domain consists of two four-strand "Greek key" beta-sheets. Although the domains are tightly anchored to one another by the hydrophobic surfaces of the two inner Greek key motifs, the N-arm, the interdomain linker and several turn regions show unexpected flexibility and disorder in solution. This may contribute entropic stabilization to the protein in solution, but may also indicate nucleation sites for unfolding or other structural transitions. The method used for solving the gammaS structure relies on the recently introduced molecular fragment replacement method, which capitalizes on the large database of protein structures previously solved by X-ray crystallography and NMR.

PubMed: 16260758
DOI: 10.1110/ps.051635205

実験手法

SOLUTION NMR