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Published online before print January 10, 2004, 10.1110/ps.03351704
Protein Science (2004), 13:549-554. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data

Deyou Zheng1,3, James M. Aramini1,3 and Gaetano T. Montelione1,2,3

1 Center for Advanced Biotechnology and Medicine (CABM) and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA
2 Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, USA
3 Northeast Structural Genomics Consortium

(RECEIVED August 2, 2003; FINAL REVISION October 14, 2003; ACCEPTED October 14, 2003)



Abstract

Staphylococcal protein A (SpA) is a virulence factor from Staphylococcus aureus that is able to bind to immunoglobulins. The 3D structures of its immunoglobulin (Ig) binding domains have been extensively studied by NMR and X-ray crystallography, and are often used as model structures in developing de novo or ab initio strategies for predicting protein structure. These small three-helix-bundle structures, reported in free proteins or Ig-bound complexes, have been determined previously using medium- to high-resolution data. Although the location and relative orientation of the three helices in most of these published 3D domain structures are consistent, there are significant differences among the reported structures regarding the tilt angle of the first helix (helix 1). We have applied residual dipolar coupling data, together with nuclear Overhauser enhancement and scalar coupling data, in refining the NMR solution structure of an engineered IgG-binding domain (Z domain) of SpA. Our results demonstrate that the three helices are almost perfectly antiparallel in orientation, with the first helix tilting slightly away from the other two helices. We propose that this high-accuracy structure of the Z domain of SpA is a more suitable target for theoretical predictions of the free domain structure than previously published lower-accuracy structures of protein A domains.

Keywords: Residual dipolar coupling; structure refinement; Z domain

Abbreviations: Ig, immunoglobulin • IgG, immunoglobulin G • RDC, residual dipolar coupling

Reprint requests to: Gaetano T. Montelione, CABM–Rutgers University, 679 Hoes Lane, Piscataway, NJ 08854, USA; e-mail: guy{at}cabm.rutgers.edu; fax: (732) 235-5633.

Afticle published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03351704.


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