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2spz

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{{STRUCTURE_2spz| PDB=2spz | SCENE= }}
{{STRUCTURE_2spz| PDB=2spz | SCENE= }}
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'''STAPHYLOCOCCAL PROTEIN A, Z-DOMAIN, NMR, 10 STRUCTURES'''
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===STAPHYLOCOCCAL PROTEIN A, Z-DOMAIN, NMR, 10 STRUCTURES===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9325113}}
==About this Structure==
==About this Structure==
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2SPZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1spz 1spz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SPZ OCA].
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2SPZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1spz 1spz]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SPZ OCA].
==Reference==
==Reference==
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[[Category: Immunoglobulin-binding protein]]
[[Category: Immunoglobulin-binding protein]]
[[Category: Three-helical bundle structure]]
[[Category: Three-helical bundle structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:21:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:12:53 2008''

Revision as of 03:12, 28 July 2008

Image:2spz.png

Template:STRUCTURE 2spz

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

Template:ABSTRACT PUBMED 9325113

About this Structure

2SPZ is a Single protein structure of sequence from Staphylococcus aureus. This structure supersedes the now removed PDB entry 1spz. Full experimental information is available from OCA.

Reference

High-resolution solution NMR structure of the Z domain of staphylococcal protein A., Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT, J Mol Biol. 1997 Oct 3;272(4):573-90. PMID:9325113

Page seeded by OCA on Mon Jul 28 06:12:53 2008

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