1q10: Difference between revisions

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-[[Image:1q10.gif|left|200px]]<br /><applet load="1q10" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1q10" />
-'''Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G'''<br />
-==Overview==
+==Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G==
-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.
+<StructureSection load='1q10' size='340' side='right'caption='[[1q10]]' scene=''>
+== Structural highlights ==
+<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='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=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>
+== Function ==
+[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
+== 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/q1/1q10_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=1q10 ConSurf].
+<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.
-==About this Structure==
+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>
-Q10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp._group_g Streptococcus sp. group g]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q10 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14516749 14516749]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1q10" style="background-color:#fffaf0;"></div>
-[[Category: Streptococcus sp. group g]]
-[[Category: Byeon, I.J.]]
-[[Category: Gronenborn, A.M.]]
-[[Category: Louis, J.M.]]
-[[Category: core mutants]]
-[[Category: domain-swapping]]
-[[Category: gb1]]
-[[Category: nmr structure]]
-[[Category: oligomerization]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:17:33 2007''
+==See Also==
+*[[Protein G|Protein G]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptococcus sp. 'group G']]
+[[Category: Byeon IJ]]
+[[Category: Gronenborn AM]]
+[[Category: Louis JM]]