3VE2: The 2.1 Angstrom Crystal Structure Of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis

Citation:
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.
PDB ID: 3VE2Download
MMDB ID: 97474
PDB Deposition Date: 2012/1/6
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 2.14  Å
Source Organism:
Similar Structures:
Biological Unit for 3VE2: tetrameric; determined by software (PISA)
Molecular Components in 3VE2
Label Count Molecule
Proteins (4 molecules)
4
Transferrin-binding Protein 2
Molecule annotation
Chemicals (40 molecules)
1
22
2
14
3
2
4
2
* Click molecule labels to explore molecular sequence information.

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