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==Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G==
==Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G==
<StructureSection load='1q10' size='340' side='right'caption='[[1q10]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
<StructureSection load='1q10' size='340' side='right'caption='[[1q10]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1q10]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsg Strsg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q10 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1q10]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q10 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;'>[[1gb1|1gb1]], [[1mpe|1mpe]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1320 STRSG])</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=1q10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q10 OCA], [https://pdbe.org/1q10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q10 RCSB], [https://www.ebi.ac.uk/pdbsum/1q10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q10 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=1q10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q10 OCA], [https://pdbe.org/1q10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q10 RCSB], [https://www.ebi.ac.uk/pdbsum/1q10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q10 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG]] Binds to the constant Fc region of IgG with high affinity.  
[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
== 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=1q10 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=1q10 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Immunoglobulin-binding domain B1 of streptococcal protein G (GB1), a small (56 residues), stable, single-domain protein, is one of the most extensively used model systems in the area of protein folding and design. Recently, NMR and X-ray structures of a quintuple GB1 core mutant (L5V/A26F/F30V/Y33F/A34F) that showed an unexpected, intertwined tetrameric architecture were determined. Here, we report the NMR structure of another mutant, derived from the tetramer by reverting the single amino acid position F26 back to the wild-type sequence A26. The structure reveals a domain-swapped dimer that involves exchange of the second beta-hairpin. The resulting overall structure comprises an eight-stranded beta-sheet whose concave side is covered by two alpha helices. The dimer dissociates into a partially folded, monomeric species with a dissociation constant of 93(+/-10)microM.
A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping.,Byeon IJ, Louis JM, Gronenborn AM J Mol Biol. 2003 Oct 10;333(1):141-52. PMID:14516749<ref>PMID:14516749</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1q10" 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: Strsg]]
[[Category: Streptococcus sp. 'group G']]
[[Category: Byeon, I J]]
[[Category: Byeon IJ]]
[[Category: Gronenborn, A M]]
[[Category: Gronenborn AM]]
[[Category: Louis, J M]]
[[Category: Louis JM]]
[[Category: Core mutant]]
[[Category: Domain-swapping]]
[[Category: Gb1]]
[[Category: Oligomerization]]
[[Category: Protein binding]]

Revision as of 09:00, 17 April 2024

Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein GEnsemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G

Structural highlights

1q10 is a 2 chain structure with sequence from Streptococcus sp. 'group G'. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPG1_STRSG Binds to the constant Fc region of IgG with high affinity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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