Ferric-binding protein

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Function

The process of bacterial multiplication requires the acquisition of growth-essential nutrients including iron, from the host cell. Ferric-binding protein (FBP) transfers iron across the periplasmic space from human transferrin to pathogenic bacteria[1].

Structural highlights

The in FBS includes with 2 tyrosine side chains (PDB code 3od7).[2] Water molecule is shown as red sphere.

Ferric-binding protein complex with Fe+3 (orange) and phosphate ion (PDB code 3od7).

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3D Structures of ferric-binding protein3D Structures of ferric-binding protein

Updated on 27-July-2020

1mrp, 3od7, 3odb – HiFBP + Fe – Haemophilus influenzae
1d9v – HiFBP
1nnf, 1qvs, 1qw0, 2o68, 2o69, 2o6a, 3kn7, 3kn8 - HiFBP (mutant) + Fe
1r1n – NgFBP + oxo-Fe – Neisseria gonorrhoeae
1xc1 – NgFBP + oxo-Zr
3tyh – NgFBP + oxo-Cu
1q35 – FBP – Mannheimia haemolytica
4elo, 4elp, 4elq – TtFBP – Thermus thermophilus
4elr – TtFBP + Fe


ReferencesReferences

  1. Chen CY, Berish SA, Morse SA, Mietzner TA. The ferric iron-binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin. Mol Microbiol. 1993 Oct;10(2):311-8. PMID:7934822
  2. Khambati HK, Moraes TF, Singh J, Shouldice SR, Yu RH, Schryvers AB. The role of vicinal tyrosine residues in the function of Haemophilus influenzae ferric binding protein A. Biochem J. 2010 Aug 27. PMID:20799927 doi:10.1042/BJ20101043

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Michal Harel, Alexander Berchansky