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4OFQ

Structure of the C-terminal domain of the Streptococcus pyogenes antigen I/II-family protein AspA

4OFQ の概要
エントリーDOI10.2210/pdb4ofq/pdb
分子名称Putative cell surface protein, CALCIUM ION (3 entities in total)
機能のキーワードbeta sandwich, adhesin, cell surface, cell adhesion
由来する生物種Streptococcus pyogenes
タンパク質・核酸の鎖数2
化学式量合計77979.53
構造登録者
Hall, M.,Nylander, A.,Jenkinson, H.F.,Persson, K. (登録日: 2014-01-15, 公開日: 2014-03-12, 最終更新日: 2024-11-27)
主引用文献Hall, M.,Nylander, S.,Jenkinson, H.F.,Persson, K.
Structure of the C-terminal domain of AspA (antigen I/II-family) protein from Streptococcus pyogenes.
FEBS Open Bio, 4:283-289, 2014
Cited by
PubMed Abstract: The pathogenic bacteria Streptococcus pyogenes can cause an array of diseases in humans, including moderate infections such as pharyngitis (strep throat) as well as life threatening conditions such as necrotizing fasciitis and puerperal fever. The antigen I/II family proteins are cell wall anchored adhesin proteins found on the surfaces of most oral streptococci and are involved in host colonization and biofilm formation. In the present study we have determined the crystal structure of the C2-3-domain of the antigen I/II type protein AspA from S. pyogenes M type 28. The structure was solved to 1.8 Å resolution and shows that the C2-3-domain is comprised of two structurally similar DEv-IgG motifs, designated C2 and C3, both containing a stabilizing covalent isopeptide bond. Furthermore a metal binding site is identified, containing a bound calcium ion. Despite relatively low sequence identity, interestingly, the overall structure shares high similarity to the C2-3-domains of antigen I/II proteins from Streptococcus gordonii and Streptococcus mutans, although certain parts of the structure exhibit distinct features. In summary this work constitutes the first step in the full structure determination of the AspA protein from S. pyogenes.
PubMed: 24918040
DOI: 10.1016/j.fob.2014.02.012
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 4ofq
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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