3VE2

The 2.1 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis

Summary for 3VE2

• Entry DOI: 10.2210/pdb3ve2/pdb
• Related: 3VE1
• Descriptor: Transferrin-binding protein 2, GLYCEROL, SULFATE ION, ... (6 entities in total)
• Functional Keywords: lipoprotein, transferrin receptor, iron acquisition, vaccine candidate, host pathogen interaction, beta barrel, receptor, transferrin, outermembrane, transferrin-binding protein
• Biological source: Neisseria meningitidis serogroup B
• Cellular location: Cell outer membrane; Lipid-anchor (Probable): Q09057
• Total number of polymer chains: 2
• Total formula weight: 144580.90

Authors

Calmettes, C.,Moraes, T.F. (deposition date: 2012-01-06, release date: 2012-02-22, Last modification date: 2024-11-06)

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

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

Experimental method

X-RAY DIFFRACTION (2.14 Å)