1edl: Difference between revisions
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==STAPHYLOCOCCAL PROTEIN A E-DOMAIN (-60), NMR, 22 STRUCTURES== | ==STAPHYLOCOCCAL PROTEIN A E-DOMAIN (-60), NMR, 22 STRUCTURES== | ||
<StructureSection load='1edl' size='340' side='right' caption='[[1edl]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1edl' size='340' side='right' caption='[[1edl]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1edl]] is a 1 chain structure | <table><tr><td colspan='2'>[[1edl]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EDL FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1edk|1edk]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1edk|1edk]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1edl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edl OCA], [http://pdbe.org/1edl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1edl RCSB], [http://www.ebi.ac.uk/pdbsum/1edl PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1edl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edl OCA], [http://pdbe.org/1edl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1edl RCSB], [http://www.ebi.ac.uk/pdbsum/1edl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1edl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1edl ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> |
Revision as of 06:57, 6 September 2017
STAPHYLOCOCCAL PROTEIN A E-DOMAIN (-60), NMR, 22 STRUCTURESSTAPHYLOCOCCAL PROTEIN A E-DOMAIN (-60), NMR, 22 STRUCTURES
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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