Ferric-binding protein

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spinqualitylabelsall models Ferric-binding protein complex with Fe+3 (orange) and phosphate ion (PDB code 3od7). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function The process of bacterial multiplication requires the acquisition of growth-essential nutrients including iron, from the host cell. Ferric-binding protein or iron binding protein or periplasmic iron 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.

3D Structures of ferric-binding protein

Updated on 26-July-2021

1mrp, 3od7, 3odb – HiFBP + Fe – Haemophilus influenzae
1d9v – HiFBP
1nnf, 1qvs, 1qw0, 2o68, 2o69, 2o6a, 3kn7, 3kn8 - HiFBP (mutant) + Fe
1o7t, 1r1n – NgFBP + oxo-Fe – Neisseria gonorrhoeae
1xc1 – NgFBP + oxo-Zr
3tyh – NgFBPA + oxo-Cu
1d9y – NgFbpA + Fe
1q35 – MhFBP – Mannheimia haemolytica
1si1 – MhFBP + Fe
4elo, 4elp, 4elq – TtFBP – Thermus thermophilus
4elr – TtFBP + Fe
6iwf – PaFBP – Pseudomonas aeruginosa
6ivy – PaFBP + Fe
6j2s – PaFBP + Ga
6mfl – FBP + Fe + acinetobactin – Acinetobacter baumannii

References

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