4WVE

Crystal structure of the Staphylococcus aureus SasG G52-E2-G53 module

4WVE の概要

• エントリーDOI: 10.2210/pdb4wve/pdb
• 関連するPDBエントリー: 3TIP 3TIQ
• 分子名称: Surface protein G, CHLORIDE ION (3 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
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : Q2G2B2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47418.51

構造登録者

Whelan, F.,Potts, J.R. (登録日: 2014-11-05, 公開日: 2015-06-03, 最終更新日: 2024-01-10)

主引用文献

Gruszka, D.T.,Whelan, F.,Farrance, O.E.,Fung, H.K.,Paci, E.,Jeffries, C.M.,Svergun, D.I.,Baldock, C.,Baumann, C.G.,Brockwell, D.J.,Potts, J.R.,Clarke, J.
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
Nat Commun, 6:7271-7271, 2015

PubMed Abstract: Bacteria exploit surface proteins to adhere to other bacteria, surfaces and host cells. Such proteins need to project away from the bacterial surface and resist significant mechanical forces. SasG is a protein that forms extended fibrils on the surface of Staphylococcus aureus and promotes host adherence and biofilm formation. Here we show that although monomeric and lacking covalent cross-links, SasG maintains a highly extended conformation in solution. This extension is mediated through obligate folding cooperativity of the intrinsically disordered E domains that couple non-adjacent G5 domains thermodynamically, forming interfaces that are more stable than the domains themselves. Thus, counterintuitively, the elongation of the protein appears to be dependent on the inherent instability of its domains. The remarkable mechanical strength of SasG arises from tandemly arrayed 'clamp' motifs within the folded domains. Our findings reveal an elegant minimal solution for the assembly of monomeric mechano-resistant tethers of variable length.

PubMed: 26027519
DOI: 10.1038/ncomms8271

実験手法

X-RAY DIFFRACTION (1.6 Å)