2J53

Solution Structure of GB1 domain Protein G and low and high pressure.

2J53 の概要

• エントリーDOI: 10.2210/pdb2j53/pdb
• 関連するPDBエントリー: 1EM7 1GB1 1IGC 1IGD 1LE3 1MPE 1MVK 1PGA 1PGB 1PGX 1PN5 1Q10 2GB1 2IGD 2IGH 2J52
• 分子名称: IMMUNOGLOBULIN G-BINDING PROTEIN G (1 entity in total)
• 機能のキーワード: peptidoglycan-anchor, immunoglobulin, pressure, cell wall, protein g, igg-binding protein
• 由来する生物種: STREPTOCOCCUS SP.
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6157.77

構造登録者

Wilton, D.J.,Tunnicliffe, R.B.,Kamatari, Y.O.,Akasaka, K.,Williamson, M.P. (登録日: 2006-09-11, 公開日: 2007-09-25, 最終更新日: 2024-05-15)

主引用文献

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

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: 18076052
DOI: 10.1002/PROT.21832

実験手法

SOLUTION NMR