Ferric-binding protein: Difference between revisions
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The <scene name='68/685614/Cv/3'>Fe atom coordination site</scene> in FBS includes with 2 tyrosine side chains (PDB code [[3od7]]).<ref>PMID:20799927</ref> Water molecule is shown as red sphere. | The <scene name='68/685614/Cv/3'>Fe atom coordination site</scene> in FBS includes with 2 tyrosine side chains (PDB code [[3od7]]).<ref>PMID:20799927</ref> Water molecule is shown as red sphere. | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of ferric-binding protein | == 3D Structures of ferric-binding protein== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} |
Revision as of 11:35, 27 July 2020
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] Water molecule is shown as red sphere. |
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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
- ↑ 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