1ZWM
NMR structure of murine gamma-S crystallin
Summary for 1ZWM
| Entry DOI | 10.2210/pdb1zwm/pdb |
| Related | 1A45 1A5D 1A7H 1AG4 1AMM 1HK0 1ZWO |
| Descriptor | Gamma crystallin S (1 entity in total) |
| Functional Keywords | alignment, deuteration, liquid crystal, pf1, relaxation, rdc, residual dipolar coupling, molecular fragment replacement, mfr, structural protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 20747.27 |
| Authors | Wu, Z.,Delaglio, F.,Wyatt, K.,Wistow, G.,Bax, A. (deposition date: 2005-06-03, release date: 2005-07-05, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 16260758DOI: 10.1110/ps.051635205 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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