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| | ==Solution structure of A219== | | ==Solution structure of A219== |
| - | <StructureSection load='1zxg' size='340' side='right'caption='[[1zxg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1zxg' size='340' side='right'caption='[[1zxg]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zxg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZXG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zxg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZXG FirstGlance]. <br> |
| - | </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=1zxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxg OCA], [http://pdbe.org/1zxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zxg RCSB], [http://www.ebi.ac.uk/pdbsum/1zxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxg ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxg OCA], [https://pdbe.org/1zxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zxg RCSB], [https://www.ebi.ac.uk/pdbsum/1zxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q53759_STAAU Q53759_STAAU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alexander, P]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Bryan, P N]] | + | [[Category: Alexander P]] |
| - | [[Category: He, Y]] | + | [[Category: Bryan PN]] |
| - | [[Category: Orban, J]] | + | [[Category: He Y]] |
| - | [[Category: Yeh, D C]] | + | [[Category: Orban J]] |
| - | [[Category: Igg-binding]]
| + | [[Category: Yeh DC]] |
| - | [[Category: Immune system-protein binding complex]]
| + | |
| - | [[Category: Phage display]]
| + | |
| - | [[Category: Protein some]]
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| Structural highlights
Function
Q53759_STAAU
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 PubMed
We describe here the solution NMR structures of two IgG binding domains with highly homologous sequences but different three-dimensional structures. The proteins, G311 and A219, are derived from the IgG binding domains of their wild-type counterparts, protein G and protein A, respectively. Through a series of site-directed mutations and phage display selections, the sequences of G311 and A219 were designed to converge to a point of high-level sequence identity while keeping their respective wild-type tertiary folds. Structures of both artificially evolved sequences were determined by NMR spectroscopy. The main chain fold of G311 can be superimposed on the wild-type alpha/beta protein G structure with a backbone rmsd of 1.4 A, and the A219 structure can be overlaid on the wild-type three-alpha-helix protein A fold also with a backbone rmsd of 1.4 A. The structure of G311, in particular, accommodates a large number of mutational changes without undergoing a change in the overall fold of the main chain. The structural differences are maintained despite a high level (59%) of sequence identity. These proteins serve as starting points for further experiments that will probe basic concepts of protein folding and conformational switching.
Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds.,He Y, Yeh DC, Alexander P, Bryan PN, Orban J Biochemistry. 2005 Nov 1;44(43):14055-61. PMID:16245921[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ He Y, Yeh DC, Alexander P, Bryan PN, Orban J. Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds. Biochemistry. 2005 Nov 1;44(43):14055-61. PMID:16245921 doi:10.1021/bi051232j
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