3TYJ

Bacillus collagen-like protein of anthracis P159S mutant

3TYJ の概要

• エントリーDOI: 10.2210/pdb3tyj/pdb
• 関連するPDBエントリー: 2R6Q 3TWI
• 分子名称: BclA protein (2 entities in total)
• 機能のキーワード: exosporium, protein binding
• 由来する生物種: Bacillus anthracis (anthrax,anthrax bacterium)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15676.68

構造登録者

Kirchdoerfer, R.N.,Herrin, B.R.,Han, B.W.,Turnbough Jr., C.L.,Cooper, M.D.,Wilson, I.A. (登録日: 2011-09-26, 公開日: 2012-03-14, 最終更新日: 2023-09-13)

主引用文献

Kirchdoerfer, R.N.,Herrin, B.R.,Han, B.W.,Turnbough, C.L.,Cooper, M.D.,Wilson, I.A.
Variable Lymphocyte Receptor Recognition of the Immunodominant Glycoprotein of Bacillus anthracis Spores.
Structure, 20:479-486, 2012

PubMed Abstract: Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA and VLRC) in function. Here, we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis, and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores.

PubMed: 22405006
DOI: 10.1016/j.str.2012.01.009

実験手法

X-RAY DIFFRACTION (2.15 Å)