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==DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G==
==DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G==
<StructureSection load='1fcl' size='340' side='right'caption='[[1fcl]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
<StructureSection load='1fcl' size='340' side='right'caption='[[1fcl]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fcl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsp Strsp]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FCL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fcl]] 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=1FCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FCL FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fd6|1fd6]], [[1gb1|1gb1]], [[1gb4|1gb4]]</div></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=1fcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcl OCA], [https://pdbe.org/1fcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fcl RCSB], [https://www.ebi.ac.uk/pdbsum/1fcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fcl ProSAT]</span></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=1fcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcl OCA], [https://pdbe.org/1fcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fcl RCSB], [https://www.ebi.ac.uk/pdbsum/1fcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fcl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1fcl ConSurf].
</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=1fcl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structures of two computationally designed core variants of the beta 1 domain of streptococcal protein G (G beta 1) were solved by (1)H NMR methods to assess the robustness of amino acid sequence selection by the ORBIT protein design package under changes in protein backbone specification. One variant has mutations at three of 10 core positions and corresponds to minimal perturbations of the native G beta 1 backbone. The other, with mutations at six of 10 positions, was calculated for a backbone in which the separation between G beta 1's alpha-helix and beta-sheet was increased by 15% relative to native G beta 1. Exchange broadening of some resonances and the complete absence of others in spectra of the sixfold mutant bespeak conformational heterogeneity in this protein. The NMR data were sufficiently abundant, however, to generate structures of similar, moderately high quality for both variants. Both proteins adopt backbone structures similar to their target folds. Moreover, the sequence selection algorithm successfully predicted all core chi(1) angles in both variants, five of six chi(2) angles in the threefold mutant and four of seven chi(2) angles in the sixfold mutant. We conclude that ORBIT calculates sequences that fold specifically to a geometry close to the template, even when the template is moderately perturbed relative to a naturally occurring structure. There are apparently limits to the size of acceptable perturbations: In this study, the larger perturbation led to undesired dynamic behavior.
Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification.,Ross SA, Sarisky CA, Su A, Mayo SL Protein Sci. 2001 Feb;10(2):450-4. PMID:11266631<ref>PMID:11266631</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fcl" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Protein G|Protein G]]
*[[Protein G|Protein G]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Strsp]]
[[Category: Streptococcus sp]]
[[Category: Mayo, S L]]
[[Category: Mayo SL]]
[[Category: Ross, S A]]
[[Category: Ross SA]]
[[Category: Sarisky, C A]]
[[Category: Sarisky CA]]
[[Category: Su, A]]
[[Category: Su A]]
[[Category: Designed core mutant]]
[[Category: Protein binding]]
[[Category: Streptococcal protein g]]

Revision as of 10:13, 20 March 2024

DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G

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