2RPV
Solution Structure of GB1 with LBT probe
Summary for 2RPV
| Entry DOI | 10.2210/pdb2rpv/pdb |
| Descriptor | Immunoglobulin G-binding protein G, LANTHANUM (III) ION (2 entities in total) |
| Functional Keywords | lanthanide binding peptide, gb1, lbt, paramagnetic effect, olivia, cell wall, igg-binding protein, peptidoglycan-anchor, secreted, immune system |
| Biological source | Streptococcus sp. group G |
| Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654 |
| Total number of polymer chains | 1 |
| Total formula weight | 8347.72 |
| Authors | Saio, T.,Ogura, K.,Yokochi, M.,Kobashigawa, Y.,Inagaki, F. (deposition date: 2008-10-28, release date: 2009-09-15, Last modification date: 2024-10-16) |
| Primary citation | Saio, T.,Ogura, K.,Yokochi, M.,Kobashigawa, Y.,Inagaki, F. Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect J.Biomol.Nmr, 44:157-166, 2009 Cited by PubMed Abstract: Paramagnetic lanthanide ions fixed in a protein frame induce several paramagnetic effects such as pseudo-contact shifts and residual dipolar couplings. These effects provide long-range distance and angular information for proteins and, therefore, are valuable in protein structural analysis. However, until recently this approach had been restricted to metal-binding proteins, but now it has become applicable to non-metalloproteins through the use of a lanthanide-binding tag. Here we report a lanthanide-binding peptide tag anchored via two points to the target proteins. Compared to conventional single-point attached tags, the two-point linked tag provides two to threefold stronger anisotropic effects. Though there is slight residual mobility of the lanthanide-binding tag, the present tag provides a higher anisotropic paramagnetic effect. PubMed: 19468839DOI: 10.1007/s10858-009-9325-z PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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