3TYJ

Bacillus collagen-like protein of anthracis P159S mutant

Summary for 3TYJ

• Entry DOI: 10.2210/pdb3tyj/pdb
• Related: 2R6Q 3TWI
• Descriptor: BclA protein (2 entities in total)
• Functional Keywords: exosporium, protein binding
• Biological source: Bacillus anthracis (anthrax,anthrax bacterium)
• Total number of polymer chains: 1
• Total formula weight: 15676.68

Authors

Kirchdoerfer, R.N.,Herrin, B.R.,Han, B.W.,Turnbough Jr., C.L.,Cooper, M.D.,Wilson, I.A. (deposition date: 2011-09-26, release date: 2012-03-14, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.15 Å)