1gb4: Difference between revisions

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-[[Image:1gb4.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1gb4", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_1gb4|  PDB=1gb4  |  SCENE=  }}
-'''HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES'''
+==HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES==
+<StructureSection load='1gb4' size='340' side='right'caption='[[1gb4]]' scene=''>
+== 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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-GB4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GB4 OCA].
+</div>
+<div class="pdbe-citations 1gb4" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Design, structure and stability of a hyperthermophilic protein variant., Malakauskas SM, Mayo SL, Nat Struct Biol. 1998 Jun;5(6):470-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9628485 9628485]
+*[[Protein G|Protein G]]
-[[Category: Single protein]]
+== References ==
-[[Category: Streptococcus sp.]]
+<references/>
-[[Category: Malakauskas, S M.]]
+__TOC__
-[[Category: Mayo, S L.]]
+</StructureSection>
-[[Category: Hyperthermophile]]
+[[Category: Large Structures]]
-[[Category: Streptococcal protein g]]
+[[Category: Streptococcus sp. G148]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:22:12 2008''
+[[Category: Malakauskas SM]]
+[[Category: Mayo SL]]