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| <StructureSection load='3fil' size='340' side='right'caption='[[3fil]], [[Resolution|resolution]] 0.88Å' scene=''> | | <StructureSection load='3fil' size='340' side='right'caption='[[3fil]], [[Resolution|resolution]] 0.88Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3fil]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsg Strsg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FIL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fil]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FIL FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.88Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2on8|2on8]], [[2onq|2onq]], [[1pga|1pga]], [[1gb4|1gb4]], [[1fcc|1fcc]], [[2qmt|2qmt]]</div></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=3fil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fil OCA], [https://pdbe.org/3fil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fil RCSB], [https://www.ebi.ac.uk/pdbsum/3fil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fil 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=3fil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fil OCA], [https://pdbe.org/3fil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fil RCSB], [https://www.ebi.ac.uk/pdbsum/3fil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fil 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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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Strsg]] | + | [[Category: Streptococcus sp. 'group G']] |
- | [[Category: Heinemann, U]] | + | [[Category: Heinemann U]] |
- | [[Category: Max, K E.A]] | + | [[Category: Max KEA]] |
- | [[Category: Alpha helix]]
| + | |
- | [[Category: Beta sheet]]
| + | |
- | [[Category: Cell wall]]
| + | |
- | [[Category: Dimerization]]
| + | |
- | [[Category: Igg-binding protein]]
| + | |
- | [[Category: Improved hydrophobic packing of core residue]]
| + | |
- | [[Category: Peptidoglycan-anchor]]
| + | |
- | [[Category: Protein binding]]
| + | |
- | [[Category: Secreted]]
| + | |
| Structural highlights
Function
SPG2_STRSG
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In previous work, a strongly stabilized variant of the beta1 domain of streptococcal protein G (Gbeta1) was obtained by an in vitro selection method. This variant, termed Gbeta1-M2, contains the four substitutions E15V, T16L, T18I, and N37L. Here we elucidated the molecular basis of the observed strong stabilizations. The contributions of these four residues were analyzed individually and in various combinations, additional selections with focused Gbeta1 gene libraries were performed, and the crystal structure of Gbeta1-M2 was determined. All single substitutions (E15V, T16L, T18I, and N37L) stabilize wild-type Gbeta1 by contributions of between 1.6 and 6.0 kJ mol(-1) (at 70 degrees C). Hydrophobic residues at positions 16 and 37 provide the major contribution to stabilization by enlarging the hydrophobic core of Gbeta1. They also increase the tendency to form dimers, as shown by dependence on the concentration of apparent molecular mass in analytical ultracentrifugation, by concentration-dependent stability, and by a strongly increased van't Hoff enthalpy of unfolding. The 0.88-A crystal structure of Gbeta1-M2 and NMR measurements in solution provide the explanation for the observed dimer formation. It involves a head-to-head arrangement of two Gbeta1-M2 molecules via six intermolecular hydrogen bonds between the two beta strands 2 and 2' and an adjacent self-complementary hydrophobic surface area, which is created by the T16L and N37L substitutions and a large 120 degrees rotation of the Tyr33 side chain. This removal of hydrophilic groups and the malleability of the created hydrophobic surface provide the basis for the dimer formation of stabilized Gbeta1 variants.
Dimer formation of a stabilized Gbeta1 variant: a structural and energetic analysis.,Thoms S, Max KE, Wunderlich M, Jacso T, Lilie H, Reif B, Heinemann U, Schmid FX J Mol Biol. 2009 Sep 4;391(5):918-32. Epub 2009 Jun 13. PMID:19527728[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thoms S, Max KE, Wunderlich M, Jacso T, Lilie H, Reif B, Heinemann U, Schmid FX. Dimer formation of a stabilized Gbeta1 variant: a structural and energetic analysis. J Mol Biol. 2009 Sep 4;391(5):918-32. Epub 2009 Jun 13. PMID:19527728 doi:10.1016/j.jmb.2009.06.031
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