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2KWD

Supramolecular Protein Structure Determination by Site-Specific Long-Range Intermolecular Solid State NMR Spectroscopy

Summary for 2KWD
Entry DOI10.2210/pdb2kwd/pdb
Related2KQ4
DescriptorImmunoglobulin G-binding protein G (1 entity in total)
Functional Keywordsgb1, crystal packing, solid-state, quaternary structure, tedor, immune system
Biological sourceStreptococcus sp. 'group G'
Cellular locationSecreted, cell wall; Peptidoglycan-anchor (Potential): P19909
Total number of polymer chains5
Total formula weight31144.05
Authors
Nieuwkoop, A.J.,Rienstra, C.M. (deposition date: 2010-04-05, release date: 2010-06-02, Last modification date: 2024-05-01)
Primary citationNieuwkoop, A.J.,Rienstra, C.M.
Supramolecular protein structure determination by site-specific long-range intermolecular solid state NMR spectroscopy.
J.Am.Chem.Soc., 132:7570-7571, 2010
Cited by
PubMed Abstract: We demonstrate that 3D Z-filtered TEDOR experiments, when performed on mixtures of isotopically labeled protein samples, report on site-specific intermolecular distance restraints. These data sets can be leveraged to perform rigorous structure calculations of the protein interface. In the example demonstrated here, we determine the packing arrangement of our nanocrystalline GB1 preparation to be consistent with the trigonal form as determined by X-ray diffraction. This represents an important proof of principle, in a case where the results can be directly compared with other structural information. We envision the application of this approach to determining the registry and quaternary arrangement of protein fibrils, which most often cannot be determined by diffraction methods.
PubMed: 20465251
DOI: 10.1021/ja100992y
PDB entries with the same primary citation
Experimental method
SOLID-STATE NMR
Structure validation

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건을2024-11-06부터공개중

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