4NSM

crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group A Streptococcus

4NSM の概要

• エントリーDOI: 10.2210/pdb4nsm/pdb
• 分子名称: Collagen-like protein SclB, SULFATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: six-helix bundle, structural protein
• 由来する生物種: Streptococcus pyogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10433.50

構造登録者

Berisio, R.,Squeglia, F.,Lukomski, S.,Bachert, B. (登録日: 2013-11-28, 公開日: 2013-12-25, 最終更新日: 2024-02-28)

主引用文献

Squeglia, F.,Bachert, B.,De Simone, A.,Lukomski, S.,Berisio, R.
The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41.
J.Biol.Chem., 289:5122-5133, 2014

PubMed Abstract: The arsenal of virulence factors deployed by streptococci includes streptococcal collagen-like (Scl) proteins. These proteins, which are characterized by a globular domain and a collagen-like domain, play key roles in host adhesion, host immune defense evasion, and biofilm formation. In this work, we demonstrate that the Scl2.3 protein is expressed on the surface of invasive M3-type strain MGAS315 of Streptococcus pyogenes. We report the crystal structure of Scl2.3 globular domain, the first of any Scl. This structure shows a novel fold among collagen trimerization domains of either bacterial or human origin. Despite there being low sequence identity, we observed that Scl2.3 globular domain structurally resembles the gp41 subunit of the envelope glycoprotein from human immunodeficiency virus type 1, an essential subunit for viral fusion to human T cells. We combined crystallographic data with modeling and molecular dynamics techniques to gather information on the entire lollipop-like Scl2.3 structure. Molecular dynamics data evidence a high flexibility of Scl2.3 with remarkable interdomain motions that are likely instrumental to the protein biological function in mediating adhesive or immune-modulatory functions in host-pathogen interactions. Altogether, our results provide molecular tools for the understanding of Scl-mediated streptococcal pathogenesis and important structural insights for the future design of small molecular inhibitors of streptococcal invasion.

PubMed: 24356966
DOI: 10.1074/jbc.M113.523597

実験手法

X-RAY DIFFRACTION (1.6 Å)