3ve2

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

Structural highlights 3ve2 is a 2 chain structure with sequence from Neimi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , Related: 3ve1 Gene: tbpB, tbp2 (NEIMI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. The structural basis of transferrin sequestration by transferrin-binding protein B.,Calmettes C, Alcantara J, Yu RH, Schryvers AB, Moraes TF Nat Struct Mol Biol. 2012 Feb 19;19(3):358-60. doi: 10.1038/nsmb.2251. PMID:22343719 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transferrin-binding protein

spinqualitylabelsall models 3ve2, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image