2WZA

Two intramolecular isopeptide bonds are identified in the crystal structure of the Streptococcus gordonii SspB C-terminal domain

2WZA の概要

• エントリーDOI: 10.2210/pdb2wza/pdb
• 関連するPDBエントリー: 2WD6 2WOY 2WQS
• 分子名称: AGGLUTININ RECEPTOR, CALCIUM ION (3 entities in total)
• 機能のキーワード: cell adhesion, cell wall, antigen i/ii, peptidoglycan-anchor
• 由来する生物種: STREPTOCOCCUS GORDONII
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : P16952
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41866.19

構造登録者

Forsgren, N.,Lamont, R.J.,Persson, K. (登録日: 2009-11-26, 公開日: 2010-02-16, 最終更新日: 2024-10-23)

主引用文献

Forsgren, N.,Lamont, R.J.,Persson, K.
Two Intramolecular Isopeptide Bonds are Identified in the Crystal Structure of the Streptococcus Gordonii Sspb C-Terminal Domain.
J.Mol.Biol., 397:740-, 2010

PubMed Abstract: Streptococcus gordonii is a primary colonizer and is involved in the formation of dental plaque. This bacterium expresses several surface proteins. One of them is the adhesin SspB, which is a member of the Antigen I/II family of proteins. SspB is a large multi-domain protein that has interactions with surface molecules on other bacteria and on host cells, and is thus a key factor in the formation of biofilms. Here, we report the crystal structure of a truncated form of the SspB C-terminal domain, solved by single-wavelength anomalous dispersion to 1.5 A resolution. The structure represents the first of a C-terminal domain from a streptococcal Antigen I/II protein and is comprised of two structurally related beta-sandwich domains, C2 and C3, both with a Ca(2+) bound in equivalent positions. In each of the domains, a covalent isopeptide bond is observed between a lysine and an asparagine, a feature that is believed to be a common stabilization mechanism in Gram-positive surface proteins. S. gordonii biofilms contain attachment sites for the periodontal pathogen Porphyromonas gingivalis and the SspB C-terminal domain has been shown to have one such recognition motif, the SspB adherence region. The motif protrudes from the protein, and serves as a handle for attachment. The structure suggests several additional putative binding surfaces, and other binding clefts may be created when the full-length protein is folded.

PubMed: 20138058
DOI: 10.1016/J.JMB.2010.01.065

実験手法

X-RAY DIFFRACTION (2.082 Å)