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< | ==HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES== | ||
<StructureSection load='1gb4' size='340' side='right'caption='[[1gb4]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gb4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._G148 Streptococcus sp. G148]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GB4 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=1gb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gb4 OCA], [https://pdbe.org/1gb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gb4 RCSB], [https://www.ebi.ac.uk/pdbsum/1gb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gb4 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/gb/1gb4_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=1gb4 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Here we report the use of an objective computer algorithm in the design of a hyperstable variant of the Streptococcal protein Gbeta1 domain (Gbeta1). The designed seven-fold mutant, Gbeta1-c3b4, has a melting temperature in excess of 100 degrees C and an enhancement in thermodynamic stability of 4.3 kcal mol(-1) at 50 degrees C over the wild-type protein. Gbeta1-c3b4 maintains the Gbeta1 fold, as determined by nuclear magnetic resonance spectroscopy, and also retains a significant level of binding to human IgG in qualitative comparisons with wild type. The basis of the stability enhancement appears to have multiple components including optimized core packing, increased burial of hydrophobic surface area, more favorable helix dipole interactions, and improvement of secondary structure propensity. The design algorithm is able to model such complex contributions simultaneously using empirical physical/chemical potential functions and a combinatorial optimization algorithm based on the dead-end elimination theorem. Because the design methodology is based on general principles, there is the potential of applying the methodology to the stabilization of other unrelated protein folds. | |||
Design, structure and stability of a hyperthermophilic protein variant.,Malakauskas SM, Mayo SL Nat Struct Biol. 1998 Jun;5(6):470-5. PMID:9628485<ref>PMID:9628485</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1gb4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Protein G|Protein G]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Streptococcus sp. G148]] | |||
[[Category: Malakauskas SM]] | |||
== | [[Category: Mayo SL]] | ||
[[Category: | |||
[[Category: Streptococcus sp.]] | |||
[[Category: Malakauskas | |||
[[Category: Mayo | |||
Latest revision as of 11:31, 22 May 2024
HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURESHYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES
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 PubMedHere we report the use of an objective computer algorithm in the design of a hyperstable variant of the Streptococcal protein Gbeta1 domain (Gbeta1). The designed seven-fold mutant, Gbeta1-c3b4, has a melting temperature in excess of 100 degrees C and an enhancement in thermodynamic stability of 4.3 kcal mol(-1) at 50 degrees C over the wild-type protein. Gbeta1-c3b4 maintains the Gbeta1 fold, as determined by nuclear magnetic resonance spectroscopy, and also retains a significant level of binding to human IgG in qualitative comparisons with wild type. The basis of the stability enhancement appears to have multiple components including optimized core packing, increased burial of hydrophobic surface area, more favorable helix dipole interactions, and improvement of secondary structure propensity. The design algorithm is able to model such complex contributions simultaneously using empirical physical/chemical potential functions and a combinatorial optimization algorithm based on the dead-end elimination theorem. Because the design methodology is based on general principles, there is the potential of applying the methodology to the stabilization of other unrelated protein folds. Design, structure and stability of a hyperthermophilic protein variant.,Malakauskas SM, Mayo SL Nat Struct Biol. 1998 Jun;5(6):470-5. PMID:9628485[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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