The 2.9 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis in complex with human transferrin

The structural basis of transferrin sequestration by transferrin-binding protein B.

Transferrin, Beta-1 metal-binding globulin, Siderophilin

0.1M sodium cacodylate pH 6.5, 14% PEG 3350, 0.1M sodium malonate, and 20% glycerol, vapor diffusion, hanging drop, temperature 293K

AUTHOR STATES THAT THE THE DIFFERENCES WITH UNP REFERENCE ARE NATURAL VARIANTS

Transferrin-binding protein 2, Serotransferrin

Transferrin receptor, iron acquisition, vaccine candidate, protein-protein complex, host pathogen interaction, Receptor, transferrin, Lipoprotein, Outermembrane protein, TRANSPORT PROTEIN
chain B and (resseq 3:212 or resseq 219:333 or resseq 337:348 or resseq 350:679 ) and (not element H) and (not element D)
chain D and (resseq 3:212 or resseq 219:333 or resseq 337:348 or resseq 350:679 ) and (not element H) and (not element D)
chain A and (resseq 39:109 or resseq 121:267 or resseq 271:297 or resseq 303:350 or resseq 376:417 or resseq 436:446 or resseq 476:499 or resseq 520:620 or resseq 629:658 or resseq 675:689 ) and (not element H) and (not element D)
chain C and (resseq 39:109 or resseq 121:267 or resseq 271:297 or resseq 303:350 or resseq 376:417 or resseq 436:446 or resseq 476:499 or resseq 520:620 or resseq 629:658 or resseq 675:689 ) and (not element H) and (not element D)