From Proteopedia
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| - | [[Image:1edj.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1edj| PDB=1edj | SCENE= }} | | {{STRUCTURE_1edj| PDB=1edj | SCENE= }} |
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| - | '''STAPHYLOCOCCAL PROTEIN A E-DOMAIN (180), NMR, 20 STRUCTURES'''
| + | ===STAPHYLOCOCCAL PROTEIN A E-DOMAIN (180), NMR, 20 STRUCTURES=== |
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| - | ==Overview==
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| - | The E-domain of staphylococcal protein A is one of five homologous IgG-binding domains designated E, D, A, B, and C that comprise the extracellular portion of protein A. The E-domain binds tightly to Fc fragments of IgG and binds certain Fv fragments with micromolar affinity. To explore further the structural features of Fc binding by protein A, and as a first step in developing a structural understanding of E-domain/Fv complex formation, we have determined the solution structure of the uncomplexed E-domain using 2D homonuclear and heteronuclear NMR spectroscopy. Complete 1H and 15N resonance assignments were obtained, and the structure was determined from 383 NOE-derived distance restrains, 34 phi and 19 chi 1 dihedral angle restraints, and 54 restraints for 27 H-bonds. 3JH alpha-H beta coupling constants and long-range NOEs involving Phe11 indicate the side chain exists in more than one conformation with differing chi 1 values. NOE restraints that were incompatible with chi 1 = -60 degrees were removed from one set of structure calculations, and those incompatible with chi 1 = 180 degrees were removed from a second set to allow Phe11 to explore both rotamer wells. Thus, two sets of 20 final structures, having no distance or dihedral angle restraint violations greater than 0.12 A or 1.6 degrees, respectively, represent the solution structure of the E-domain. Backbone atomic rms differences with respect to the mean coordinates for each set of 20 structures for residues 8-53 averaged 0.41 +/- 0.06 and 0.35 +/- 0.06 A. No significant differences in the overall structure result from the different orientations of Phe11. The solution structure of the E-domain consists of three alpha-helices that pack together to form a compact helical bundle. A detailed comparison between the E-domain ensembles and the previously determined structure for the B-domain in complex with Fc indicates that only the 180 degrees chi 1 rotamer of Phe11 is competent for binding; the -60 degrees chi 1 rotamer must reorient to 180 degrees to create a cavity that is filled by Ile253 from the CH2 domain of Fc in the Fc-bound complex. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8952510}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8952510 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8952510}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1EDJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDJ OCA]. | + | 1EDJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDJ OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Signal]] | | [[Category: Signal]] |
| | [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:57:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:31:57 2008'' |
Revision as of 21:32, 30 June 2008
Template:STRUCTURE 1edj
STAPHYLOCOCCAL PROTEIN A E-DOMAIN (180), NMR, 20 STRUCTURES
Template:ABSTRACT PUBMED 8952510
About this Structure
1EDJ is a Single protein structure of sequence from Staphylococcus aureus. Full experimental information is available from OCA.
Reference
Solution structure of the E-domain of staphylococcal protein A., Starovasnik MA, Skelton NJ, O'Connell MP, Kelley RF, Reilly D, Fairbrother WJ, Biochemistry. 1996 Dec 3;35(48):15558-69. PMID:8952510
Page seeded by OCA on Tue Jul 1 00:31:57 2008
