Ferric-binding protein: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The <scene name='68/685614/Cv/2'>Fe atom coordination site</scene> in FBS includes 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 (PDB code [[3od7]]).<ref>PMID:20799927</ref> | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of ferric-binding protein'== | == 3D Structures of ferric-binding protein'== | ||
Revision as of 15:29, 25 January 2016
FunctionThe 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 highlightsThe in FBS includes with 2 tyrosine side chains (PDB code 3od7).[2] |
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3D Structures of ferric-binding protein'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
ReferencesReferences
- ↑ 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
- ↑ 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