PDBsum entry 1zwm

Structural protein

PDB id: 1zwm

Contents

Protein chain

177 a.a. *

* Residue conservation analysis

PDB id:

1zwm

Name:

Structural protein

Title:

Nmr structure of murine gamma-s crystallin

Structure:

Gamma crystallin s. Chain: a. Synonym: gamma crystallin s. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: crygs. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

20 models

Authors:

Z.Wu,F.Delaglio,K.Wyatt,G.Wistow,A.Bax

Key ref:

Z.Wu et al. (2005). Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR. Protein Sci, 14, 3101-3114. PubMed id: 16260758 DOI: 10.1110/ps.051635205

Date:

03-Jun-05 Release date: 05-Jul-05

Protein chain

O35486  (CRBS_MOUSE) -  Gamma-crystallin S from Mus musculus

Seq: 178 a.a.

Struc: 177 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1110/ps.051635205

Protein Sci 14:3101-3114 (2005)

PubMed id: 16260758

Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.

Z.Wu, F.Delaglio, K.Wyatt, G.Wistow, A.Bax.

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.

Selected figure(s)

Figure 4.
Figure 4. Ribbon diagram of the NMR structure of S. Methyl-methyl NOEs at the domain interface are marked by red arrows. A subset of the long-range HN-HN NOEs is marked by blue arrows. Figure was prepared with the program Molmol (Koradi et al. 1996).

Figure 5.
Figure 5. Backbone superposition of the 10 lowest energy S NMR structures (blue), and the crystal structures of B (red; PDB entry 1AMM [PDB] ) and D (green; 1HK0). Superposition corresponds to a best fit for corresponding backbone atoms of the N-terminal domain (bottom of figure). Gray residues in the NMR structure correspond to those for which conformational exchange resulted in missing backbone amide signals. The increased distance between N- and C-terminal domains relative to the X-ray structures in all likelihood is an artifact resulting from insufficient interdomain NOEs.

The above figures are reprinted by permission from the Protein Society: Protein Sci (2005, 14, 3101-3114) copyright 2005.

Figures were selected by an automated process.