3VE1

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

Summary for 3VE1

Entry DOI	10.2210/pdb3ve1/pdb
Related	3VE2
Descriptor	Transferrin-binding protein 2, Serotransferrin, GLYCEROL, ... (6 entities in total)
Functional Keywords	transferrin receptor, iron acquisition, vaccine candidate, protein-protein complex, host pathogen interaction, receptor, transferrin, lipoprotein, outermembrane protein, transport protein
Biological source	Neisseria meningitidis serogroup B More
Cellular location	Cell outer membrane; Lipid-anchor (Probable): Q09057 Secreted: P02787
Total number of polymer chains	4
Total formula weight	294815.21
Authors	Calmettes, C.,Moraes, T.F. (deposition date: 2012-01-06, release date: 2012-02-22, Last modification date: 2013-09-18)
Primary citation	Calmettes, C.,Alcantara, J.,Yu, R.H.,Schryvers, A.B.,Moraes, T.F. The structural basis of transferrin sequestration by transferrin-binding protein B. Nat.Struct.Mol.Biol., 19:358-360, 2012 Cited by PubMed Abstract: Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin during infection through a surface transferrin receptor system composed of proteins TbpA and TbpB. Here we present the crystal structures of TbpB from N. meningitidis in its apo form and in complex with human transferrin. The structure reveals how TbpB sequesters and initiates iron release from human transferrin. PubMed: 22343719 DOI: 10.1038/nsmb.2251 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.956 Å)

Structure validation