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| | <StructureSection load='6cne' size='340' side='right'caption='[[6cne]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='6cne' size='340' side='right'caption='[[6cne]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strsg Strsg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CNE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cne]] 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=6CNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CNE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spg ([http://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=6cne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cne OCA], [https://pdbe.org/6cne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cne RCSB], [https://www.ebi.ac.uk/pdbsum/6cne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cne ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cne OCA], [http://pdbe.org/6cne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cne RCSB], [http://www.ebi.ac.uk/pdbsum/6cne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cne ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6cne" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6cne" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Protein G|Protein G]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strsg]] | + | [[Category: Streptococcus sp. 'group G']] |
| - | [[Category: Chen, Q]] | + | [[Category: Chen Q]] |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunoglobulin g-binding protein domain b1]]
| + | |
| Structural highlights
Function
SPG1_STRSG Binds to the constant Fc region of IgG with high affinity.
Publication Abstract from PubMed
Sulfur is critical for the correct structure and proper function of proteins. Yet, lacking a sensitive enough isotope, nuclear magnetic resonance (NMR) experiments are unable to deliver for sulfur in proteins the usual wealth of chemical, dynamic, and structural information. This limitation can be circumvented by substituting sulfur with selenium, which has similar physicochemical properties and minimal impact on protein structures but possesses an NMR compatible isotope ((77)Se). Here we exploit the sensitivity of (77)Se NMR to the nucleus' chemical milieu and use selenomethionine as a probe for its proteinaceous environment. However, such selenium NMR spectra of proteins currently resist a reliable interpretation because systematic connections between variations of system variables and changes in (77)Se NMR parameters are still lacking. To start narrowing this knowledge gap, we report here on a biological (77)Se magnetic resonance data bank based on a systematically designed library of GB1 variants in which a single selenomethionine was introduced at different locations within the protein. We recorded the resulting isotropic (77)Se chemical shifts and relaxation times for six GB1 variants by solution-state (77)Se NMR. For four of the GB1 variants we were also able to determine the chemical shift anisotropy tensor of SeM by solid-state (77)Se NMR. To enable interpretation of the NMR data, the structures of five of the GB1 variants were solved by X-ray crystallography to a resolution of 1.2 A, allowing us to unambiguously determine the conformation of the selenomethionine. Finally, we combine our solution- and solid-state NMR data with the structural information to arrive at general insights regarding the execution and interpretation of (77)Se NMR experiments that exploit selenomethionine to probe proteins.
(77)Se NMR Probes the Protein Environment of Selenomethionine.,Chen Q, Xu S, Lu X, Boeri MV, Pepelyayeva Y, Diaz EL, Soni SD, Allaire M, Forstner MB, Bahnson BJ, Rozovsky S J Phys Chem B. 2020 Jan 7. doi: 10.1021/acs.jpcb.9b07466. PMID:31846581[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen Q, Xu S, Lu X, Boeri MV, Pepelyayeva Y, Diaz EL, Soni SD, Allaire M, Forstner MB, Bahnson BJ, Rozovsky S. (77)Se NMR Probes the Protein Environment of Selenomethionine. J Phys Chem B. 2020 Jan 7. doi: 10.1021/acs.jpcb.9b07466. PMID:31846581 doi:http://dx.doi.org/10.1021/acs.jpcb.9b07466
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