5DBL

Crystal structure of the Staphylococcus aureus SasG E1-G52 Y625W mutant

5DBL の概要

• エントリーDOI: 10.2210/pdb5dbl/pdb
• 関連するPDBエントリー: 3TIP
• 分子名称: Surface protein G (2 entities in total)
• 機能のキーワード: sasg, biofilm, staphylococcus aureus, 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: 1
• 化学式量合計: 14516.24

構造登録者

Whelan, F.,Potts, J.R. (登録日: 2015-08-21, 公開日: 2016-09-28, 最終更新日: 2024-01-10)

主引用文献

Gruszka, D.T.,Mendonca, C.A.,Paci, E.,Whelan, F.,Hawkhead, J.,Potts, J.R.,Clarke, J.
Disorder drives cooperative folding in a multidomain protein.
Proc.Natl.Acad.Sci.USA, 113:11841-11846, 2016

PubMed Abstract: Many human proteins contain intrinsically disordered regions, and disorder in these proteins can be fundamental to their function-for example, facilitating transient but specific binding, promoting allostery, or allowing efficient posttranslational modification. SasG, a multidomain protein implicated in host colonization and biofilm formation in Staphylococcus aureus, provides another example of how disorder can play an important role. Approximately one-half of the domains in the extracellular repetitive region of SasG are intrinsically unfolded in isolation, but these E domains fold in the context of their neighboring folded G5 domains. We have previously shown that the intrinsic disorder of the E domains mediates long-range cooperativity between nonneighboring G5 domains, allowing SasG to form a long, rod-like, mechanically strong structure. Here, we show that the disorder of the E domains coupled with the remarkable stability of the interdomain interface result in cooperative folding kinetics across long distances. Formation of a small structural nucleus at one end of the molecule results in rapid structure formation over a distance of 10 nm, which is likely to be important for the maintenance of the structural integrity of SasG. Moreover, if this normal folding nucleus is disrupted by mutation, the interdomain interface is sufficiently stable to drive the folding of adjacent E and G5 domains along a parallel folding pathway, thus maintaining cooperative folding.

PubMed: 27698144
DOI: 10.1073/pnas.1608762113

実験手法

X-RAY DIFFRACTION (1.6 Å)