4NPF

High-resolution structure of two tandem B domains of staphylococcal protein A connected by the conserved linker

4NPF の概要

• エントリーDOI: 10.2210/pdb4npf/pdb
• 関連するPDBエントリー: 4NPD 4NPE
• 分子名称: Immunoglobulin G-binding protein A (2 entities in total)
• 機能のキーワード: spa, three-helix bundle, conformational heterogeneity, rapidly unfolding and folding, ruf, antibody binding, antibody, tnfr1, von willebrand factor, protein binding
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : P38507
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26545.06

構造登録者

Deis, L.N.,Pemble IV, C.W.,Oas, T.G.,Richardson, J.S.,Richardson, D.C. (登録日: 2013-11-21, 公開日: 2014-10-08, 最終更新日: 2024-02-28)

主引用文献

Deis, L.N.,Pemble, C.W.,Qi, Y.,Hagarman, A.,Richardson, D.C.,Richardson, J.S.,Oas, T.G.
Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity.
Structure, 22:1467-1477, 2014

PubMed Abstract: The Staphylococcus aureus virulence factor staphylococcal protein A (SpA) is a major contributor to bacterial evasion of the host immune system, through high-affinity binding to host proteins such as antibodies. SpA includes five small three-helix-bundle domains (E-D-A-B-C) separated by conserved flexible linkers. Prior attempts to crystallize individual domains in the absence of a binding partner have apparently been unsuccessful. There have also been no previous structures of tandem domains. Here we report the high-resolution crystal structures of a single C domain, and of two B domains connected by the conserved linker. Both structures exhibit extensive multiscale conformational heterogeneity, which required novel modeling protocols. Comparison of domain structures shows that helix1 orientation is especially heterogeneous, coordinated with changes in side chain conformational networks and contacting protein interfaces. This represents the kind of structural plasticity that could enable SpA to bind multiple partners.

PubMed: 25295398
DOI: 10.1016/j.str.2014.08.014

実験手法

X-RAY DIFFRACTION (1.49 Å)