3TIP

Crystal structure of Staphylococcus aureus SasG E-G52 module

3TIP の概要

• エントリーDOI: 10.2210/pdb3tip/pdb
• 関連するPDBエントリー: 3TIQ
• 分子名称: Surface protein G (2 entities in total)
• 機能のキーワード: single-layer beta sheet, biofilm formation, surface, structural protein
• 由来する生物種: Staphylococcus aureus subsp. aureus
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : Q2G2B2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14493.20

構造登録者

Gruszka, D.T.,Wojdyla, J.A.,Turkenburg, J.P.,Potts, J.R. (登録日: 2011-08-21, 公開日: 2012-04-18, 最終更新日: 2024-02-28)

主引用文献

Gruszka, D.T.,Wojdyla, J.A.,Bingham, R.J.,Turkenburg, J.P.,Manfield, I.W.,Steward, A.,Leech, A.P.,Geoghegan, J.A.,Foster, T.J.,Clarke, J.,Potts, J.R.
Staphylococcal biofilm-forming protein has a contiguous rod-like structure.
Proc.Natl.Acad.Sci.USA, 109:E1011-E1018, 2012

PubMed Abstract: Staphylococcus aureus and Staphylococcus epidermidis form communities (called biofilms) on inserted medical devices, leading to infections that affect many millions of patients worldwide and cause substantial morbidity and mortality. As biofilms are resistant to antibiotics, device removal is often required to resolve the infection. Thus, there is a need for new therapeutic strategies and molecular data that might assist their development. Surface proteins S. aureus surface protein G (SasG) and accumulation-associated protein (S. epidermidis) promote biofilm formation through their "B" regions. B regions contain tandemly arrayed G5 domains interspersed with approximately 50 residue sequences (herein called E) and have been proposed to mediate intercellular accumulation through Zn(2+)-mediated homodimerization. Although E regions are predicted to be unstructured, SasG and accumulation-associated protein form extended fibrils on the bacterial surface. Here we report structures of E-G5 and G5-E-G5 from SasG and biophysical characteristics of single and multidomain fragments. E sequences fold cooperatively and form interlocking interfaces with G5 domains in a head-to-tail fashion, resulting in a contiguous, elongated, monomeric structure. E and G5 domains lack a compact hydrophobic core, and yet G5 domain and multidomain constructs have thermodynamic stabilities only slightly lower than globular proteins of similar size. Zn(2+) does not cause SasG domains to form dimers. The work reveals a paradigm for formation of fibrils on the 100-nm scale and suggests that biofilm accumulation occurs through a mechanism distinct from the "zinc zipper." Finally, formation of two domains by each repeat (as in SasG) might reduce misfolding in proteins when the tandem arrangement of highly similar sequences is advantageous.

PubMed: 22493247
DOI: 10.1073/pnas.1119456109

実験手法

X-RAY DIFFRACTION (1.7009 Å)