Transferrin-binding protein

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Revision as of 10:09, 24 January 2017

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Transferrin-binding protein (Tbp) is a surface-exposed lipoprotein which is part of the transferrin receptor. The transferrin receptor functions in acquiring iron for some pathogenic Gram-negative bacteria[1]. Structural highlights

3D structures of transferrin-binding protein

Updated on 24-January-2017

3v8x, 3s9l, 3s9m, 3s9n – NmTbpA + serotransferrin – Neisseria meningitis
3v89 – NmTbpA C-terminal + serotransferrin
4qq1, 3ve2, 3v8u – NmTbpB
4u9c – NmTbpB N-terminal
3ve1 – NmTbpB + serotransferrin
4o3w – AsTbpB (mutant) – Actinobacillus suis
3pqu – AsTbpB
4o3x, 4o3y, 4o3z, 4o49 – ApTbpB (mutant) – Actinobacillus pleuropneumoniae
3hoe – ApTbpB N-terminal
3hol, 3pqs – ApTbpB
4o4u, 4o4x – TbpB (mutant) – Haemophilus parasuis

References

1. ↑ Nemish U, Yu RH, Tari LW, Krewulak K, Schryvers AB. The bacterial receptor protein, transferrin-binding protein B, does not independently facilitate the release of metal ion from human transferrin. Biochem Cell Biol. 2003 Aug;81(4):275-83. PMID:14569300 doi:http://dx.doi.org/10.1139/o03-057