2SPZ

STAPHYLOCOCCAL PROTEIN A, Z-DOMAIN, NMR, 10 STRUCTURES

Replaces:  1SPZ

Summary for 2SPZ

• Entry DOI: 10.2210/pdb2spz/pdb
• NMR Information: BMRB: 4023
• Descriptor: IMMUNOGLOBULIN G BINDING PROTEIN A (1 entity in total)
• Functional Keywords: immunoglobulin-binding protein, three-helical bundle structure, immune system
• Biological source: Staphylococcus aureus
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): P38507
• Total number of polymer chains: 1
• Total formula weight: 6648.32

Authors

Montelione, G.T.,Tashiro, M.,Tejero, R.,Lyons, B.A. (deposition date: 1998-07-29, release date: 1998-08-05, Last modification date: 2024-05-22)

Primary citation

Tashiro, M.,Tejero, R.,Zimmerman, D.E.,Celda, B.,Nilsson, B.,Montelione, G.T.
High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
J.Mol.Biol., 272:573-590, 1997

PubMed Abstract: Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are targets for protein engineering efforts and for the development of computational approaches for de novo protein folding. The NMR solution structure of an engineered IgG-binding domain of SpA, the Z domain (an analog of the B domain of SpA), has been determined by simulated annealing with restrained molecular dynamics on the basis of 671 conformational constraints. The Z domain contains three well-defined alpha-helices corresponding to polypeptide segments Lys7 to Leu17 (helix 1), Glu24 to Asp36 (helix 2), and Ser41 to Ala54 (helix 3). A family of ten conformers representing the solution structure of the Z domain was computed by simulated annealing of restrained molecular dynamics using the program CONGEN. The average of the root-mean-square deviations (r.m. s.d.) of the individual NMR conformers, relative to the mean coordinates, for the backbone atoms N, Calpha and C' of residues Phe5 through Ala56 is 0.69 A; the corresponding backbone r.m.s.d. for the three-helical core is 0.44 A. Helices 1, 2 and 3 are antiparallel in orientation (Omega12=-170(+/-4) degrees , Omega13=+16(+/-3) degrees , Omega23=+173(+/-7) degrees ). A comparison of backbone amide hydrogen/deuterium exchange rates in free and IgG-bound Z domains demonstrates that the amide protons of helices 1, 2 and 3 are protected from rapid exchange in both states, indicating that all three helices are also intact in the IgG-bound state. These solution NMR results differ from the previously determined X-ray structure of the similar SpA B domain in complex with the Fc fragment of a human IgG antibody, where helix 3 is not observed in the electron density map and from the solution NMR structure of the B domain, where helix 3 is observed but helix 1 is tilted by approximately 30 degrees with respect to helices 2 and 3. Hydrogen-bonded N-cap and C-cap formation is observed for all three helices of the Z domain; these capping interactions appear to be highly conserved in the five homologous domains of SpA.

PubMed: 9325113
DOI: 10.1006/jmbi.1997.1265

Experimental method

SOLUTION NMR