1zxh: Difference between revisions
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==G311 mutant protein== | |||
<StructureSection load='1zxh' size='340' side='right'caption='[[1zxh]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zxh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZXH FirstGlance]. <br> | |||
</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=1zxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxh OCA], [https://pdbe.org/1zxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zxh RCSB], [https://www.ebi.ac.uk/pdbsum/1zxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zx/1zxh_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=1zxh ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:16245921</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zxh" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Protein G|Protein G]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Streptococcus sp | </StructureSection> | ||
[[Category: Alexander | [[Category: Large Structures]] | ||
[[Category: Bryan | [[Category: Streptococcus sp]] | ||
[[Category: He | [[Category: Alexander P]] | ||
[[Category: Orban | [[Category: Bryan PN]] | ||
[[Category: Yeh | [[Category: He Y]] | ||
[[Category: Orban J]] | |||
[[Category: Yeh DC]] | |||
Latest revision as of 12:21, 22 May 2024
G311 mutant proteinG311 mutant protein
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. See AlsoReferences
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