HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Research Data All Versions of this Article: ps.051635205v1 14/12/3101    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wu, Z. Articles by Bax, A. Search for Related Content PubMed PubMed Citation Articles by Wu, Z. Articles by Bax, A. Social Bookmarking                   What's this?

Solution structure of S-crystallin by molecular fragment replacement NMR

¹ Laboratory of Chemical Physics, NIDDK, and ² Section on Molecular Structure and Functional Genomics, NEI, National Institutes of Health, Bethesda, Maryland 20892, USA
³ Biochemistry Department, Ohio State University, Columbus, Ohio 43210, USA

(RECEIVED June 6, 2005; FINAL REVISION September 2, 2005; ACCEPTED September 4, 2005)

The solution structure of murine S-crystallin (S) 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. S consists of two topologically similar domains, arranged with an approximate twofold symmetry, and each domain shows close structural homology to closely related (~50% sequence identity) domains found in other members of the -crystallin family. Each domain consists of two four-strand "Greek key" -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 S 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.

Keywords: alignment; deuteration; liquid crystal; Pf1; relaxation; RDC; residual dipolar coupling; structural proteins; NMR spectroscopy; heteronuclear NMR; new methods; database mining

Abbreviations: MFR, molecular fragment replacement • S, murine S-crystallin • D_a, magnitude of the dipolar coupling tensor • R, rhombicity of the dipolar coupling tensor

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051635205.

Reprint requests to: Ad Bax, Building 5, Room 126, NIH, Bethesda, MD 20892-0520, USA; e-mail: bax{at}nih.gov; fax: (301) 402-0907.

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				I. A. Mills, S. L. Flaugh, M. S. Kosinski-Collins, and J. A. King Folding and stability of the isolated Greek key domains of the long-lived human lens proteins {gamma}D-crystallin and {gamma}S-crystallin Protein Sci., November 1, 2007; 16(11): 2427 - 2444. [Abstract] [Full Text] [PDF]