2J53
Solution Structure of GB1 domain Protein G and low and high pressure.
Summary for 2J53
| Entry DOI | 10.2210/pdb2j53/pdb |
| Related | 1EM7 1GB1 1IGC 1IGD 1LE3 1MPE 1MVK 1PGA 1PGB 1PGX 1PN5 1Q10 2GB1 2IGD 2IGH 2J52 |
| Descriptor | IMMUNOGLOBULIN G-BINDING PROTEIN G (1 entity in total) |
| Functional Keywords | peptidoglycan-anchor, immunoglobulin, pressure, cell wall, protein g, igg-binding protein |
| Biological source | STREPTOCOCCUS SP. |
| Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654 |
| Total number of polymer chains | 1 |
| Total formula weight | 6157.77 |
| Authors | Wilton, D.J.,Tunnicliffe, R.B.,Kamatari, Y.O.,Akasaka, K.,Williamson, M.P. (deposition date: 2006-09-11, release date: 2007-09-25, Last modification date: 2024-05-15) |
| Primary citation | Wilton, D.J.,Tunnicliffe, R.B.,Kamatari, Y.O.,Akasaka, K.,Williamson, M.P. Pressure-Induced Changes in the Solution Structure of the Gb1 Domain of Protein G. Proteins, 71:1432-, 2008 Cited by PubMed Abstract: The solution structure of the GB1 domain of protein G at a pressure of 2 kbar is presented. The structure was calculated as a change from an energy-minimised low-pressure structure using (1)H chemical shifts. Two separate changes can be characterised: a compression/distortion, which is linear with pressure; and a stabilisation of an alternative folded state. On application of pressure, linear chemical shift changes reveal that the backbone structure changes by about 0.2 A root mean square, and is compressed by about 1% overall. The alpha-helix compresses, particularly at the C-terminal end, and moves toward the beta-sheet, while the beta-sheet is twisted, with the corners closest to the alpha-helix curling up towards it. The largest changes in structure are along the second beta-strand, which becomes more twisted. This strand is where the protein binds to IgG. Curved chemical shift changes with pressure indicate that high pressure also populates an alternative structure with a distortion towards the C-terminal end of the helix, which is likely to be caused by insertion of a water molecule. PubMed: 18076052DOI: 10.1002/PROT.21832 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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