1q2n
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REFINED Solution NMR structure of the Z domain of STAPHYLOCOCCAL PROTEIN A
OverviewOverview
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.
About this StructureAbout this Structure
1Q2N is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
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., Zheng D, Aramini JM, Montelione GT, Protein Sci. 2004 Feb;13(2):549-54. Epub 2004 Jan 10. PMID:14718654
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