4IGB

Crystal structure of the N-terminal domain of the Streptococcus gordonii adhesin Sgo0707

4IGB の概要

• エントリーDOI: 10.2210/pdb4igb/pdb
• 分子名称: LPXTG cell wall surface protein, SULFATE ION, GLYCEROL, ... (9 entities in total)
• 機能のキーワード: beta-sandwich folds, adhesin, collagen-binding, oral keratinocytes, cell wall anchored protein, cell adhesion
• 由来する生物種: Streptococcus gordonii; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 193951.46

構造登録者

Nylander, A.,Svensater, G.,Senadheera, D.B.,Cvitkovitch, D.G.,Davies, J.R.,Persson, K. (登録日: 2012-12-17, 公開日: 2013-06-05, 最終更新日: 2024-03-20)

主引用文献

Nylander, A.,Svensater, G.,Senadheera, D.B.,Cvitkovitch, D.G.,Davies, J.R.,Persson, K.
Structural and Functional Analysis of the N-terminal Domain of the Streptococcus gordonii Adhesin Sgo0707
Plos One, 8:e63768-e63768, 2013

PubMed Abstract: The commensal Streptococcus gordonii expresses numerous surface adhesins with which it interacts with other microorganisms, host cells and salivary proteins to initiate dental plaque formation. However, this Gram-positive bacterium can also spread to non-oral sites such as the heart valves and cause infective endocarditis. One of its surface adhesins, Sgo0707, is a large protein composed of a non-repetitive N-terminal region followed by several C-terminal repeat domains and a cell wall sorting motif. Here we present the crystal structure of the Sgo0707 N-terminal domains, refined to 2.1 Å resolution. The model consists of two domains, N1 and N2. The largest domain, N1, comprises a putative binding cleft with a single cysteine located in its centre and exhibits an unexpected structural similarity to the variable domains of the streptococcal Antigen I/II adhesins. The N2-domain has an IgG-like fold commonly found among Gram-positive surface adhesins. Binding studies performed on S. gordonii wild-type and a Sgo0707 deficient mutant show that the Sgo0707 adhesin is involved in binding to type-1 collagen and to oral keratinocytes.

PubMed: 23691093
DOI: 10.1371/journal.pone.0063768

実験手法

X-RAY DIFFRACTION (2.09 Å)