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| | ==Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy== | | ==Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy== |
| - | <StructureSection load='2kq4' size='340' side='right' caption='[[2kq4]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2kq4' size='340' side='right'caption='[[2kq4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kq4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strsg Strsg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KQ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KQ4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kq4]] is a 1 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=2KQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KQ4 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=2kq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kq4 OCA], [http://pdbe.org/2kq4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kq4 RCSB], [http://www.ebi.ac.uk/pdbsum/2kq4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kq4 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=2kq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kq4 OCA], [https://pdbe.org/2kq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kq4 RCSB], [https://www.ebi.ac.uk/pdbsum/2kq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kq4 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strsg]] | + | [[Category: Large Structures]] |
| - | [[Category: Franks, W]] | + | [[Category: Streptococcus sp. 'group G']] |
| - | [[Category: Nieuwkoop, A J]]
| + | [[Category: Franks W]] |
| - | [[Category: Rienstra, C M]]
| + | [[Category: Nieuwkoop AJ]] |
| - | [[Category: Shah, G J]]
| + | [[Category: Rienstra CM]] |
| - | [[Category: Wylie, B J]] | + | [[Category: Shah GJ]] |
| - | [[Category: Cell wall]] | + | [[Category: Wylie BJ]] |
| - | [[Category: Gb1]] | + | |
| - | [[Category: Igg-binding protein]] | + | |
| - | [[Category: Immune system]] | + | |
| - | [[Category: Peptidoglycan-anchor]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Solid-state]]
| + | |
| - | [[Category: Tedor]]
| + | |
| - | [[Category: Thermostable]]
| + | |
| 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
We show that quantitative internuclear (15)N-(13)C distances can be obtained in sufficient quantity to determine a complete, high-resolution structure of a moderately sized protein by magic-angle spinning solid-state NMR spectroscopy. The three-dimensional ZF-TEDOR pulse sequence is employed in combination with sparse labeling of (13)C sites in the beta1 domain of the immunoglobulin binding protein G (GB1), as obtained by bacterial expression with 1,3-(13)C or 2-(13)C-glycerol as the (13)C source. Quantitative dipolar trajectories are extracted from two-dimensional (15)N-(13)C planes, in which approximately 750 cross peaks are resolved. The experimental data are fit to exact theoretical trajectories for spin clusters (consisting of one (13)C and several (15)N each), yielding quantitative precision as good as 0.1 A for approximately 350 sites, better than 0.3 A for another 150, and approximately 1.0 A for 150 distances in the range of 5-8 A. Along with isotropic chemical shift-based (TALOS) dihedral angle restraints, the distance restraints are incorporated into simulated annealing calculations to yield a highly precise structure (backbone RMSD of 0.25+/-0.09 A), which also demonstrates excellent agreement with the most closely related crystal structure of GB1 (2QMT, bbRMSD 0.79+/-0.03 A). Moreover, side chain heavy atoms are well restrained (0.76+/-0.06 A total heavy atom RMSD). These results demonstrate for the first time that quantitative internuclear distances can be measured throughout an entire solid protein to yield an atomic-resolution structure.
Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy.,Nieuwkoop AJ, Wylie BJ, Franks WT, Shah GJ, Rienstra CM J Chem Phys. 2009 Sep 7;131(9):095101. PMID:19739873[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nieuwkoop AJ, Wylie BJ, Franks WT, Shah GJ, Rienstra CM. Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy. J Chem Phys. 2009 Sep 7;131(9):095101. PMID:19739873 doi:10.1063/1.3211103
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