Ferric-binding protein

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	== Structural highlights ==		== Structural highlights ==
-	The Fe atom in FBS is coordinated with 2 tyrosine side chains.	+	The <scene name='68/685614/Cv/2'>Fe atom coordination site</scene> in FBS includes with 2 tyrosine side chains.
	</StructureSection>		</StructureSection>
	== 3D Structures of ferric-binding protein'==		== 3D Structures of ferric-binding protein'==

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Revision as of 12:27, 25 January 2016

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 (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.

3D Structures of ferric-binding protein'

Updated on 25-January-2016

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

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