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Ferric-binding protein
From Proteopedia
(New page: <StructureSection load='3od7' size='340' side='right' caption='Ferric-binding protein complex with Fe+3 (PDB code 3od7).' scene=''> == Function == The process of bacterial multiplica...) |
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| - | + | <StructureSection load='3od7' size='350' side='right' caption='Ferric-binding protein complex with Fe+3 (orange) and phosphate ion (PDB code [[3od7]]).' scene='68/685614/Cv/1'> | |
| - | <StructureSection load='3od7' size=' | + | |
== Function == | == 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. | + | 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<ref>PMID:7934822</ref>. |
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== Structural highlights == | == Structural highlights == | ||
| - | + | 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}} | ||
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[[1d9v]] – HiFBP <br /> | [[1d9v]] – HiFBP <br /> | ||
[[1nnf]], [[1qvs]], [[1qw0]], [[2o68]], [[2o69]], [[2o6a]], [[3kn7]], [[3kn8]] - HiFBP (mutant) + Fe <br /> | [[1nnf]], [[1qvs]], [[1qw0]], [[2o68]], [[2o69]], [[2o6a]], [[3kn7]], [[3kn8]] - HiFBP (mutant) + Fe <br /> | ||
| - | [[ | + | [[1o7t]], [[1r1n]] – NgFBP + oxo-Fe – ''Neisseria gonorrhoeae''<br /> |
| - | [[1xc1]] – NgFBP + oxo- | + | [[1xc1]] – NgFBP + oxo-Zr<br /> |
| - | [[3tyh]] – | + | [[3tyh]] – NgFBPA + oxo-Cu<br /> |
| + | [[1d9y]] – NgFbpA + Fe<br /> | ||
| + | [[1q35]] – MhFBP – ''Mannheimia haemolytica''<br /> | ||
| + | [[1si1]] – MhFBP + Fe<br /> | ||
| + | [[4elo]], [[4elp]], [[4elq]] – TtFBP – ''Thermus thermophilus''<br /> | ||
| + | [[4elr]] – TtFBP + Fe<br /> | ||
| + | [[6iwf]] – PaFBP – ''Pseudomonas aeruginosa''<br /> | ||
| + | [[6ivy]] – PaFBP + Fe <br /> | ||
| + | [[6j2s]] – PaFBP + Ga<br /> | ||
| + | [[6mfl]] – FBP + Fe + acinetobactin – ''Acinetobacter baumannii''<br /> | ||
| + | [[1y4t]], [[3e13]] – FBP + Fe – ''Campylobacter jejuni''<br /> | ||
| + | [[7li0]], [[7li1]] – FBP + Fe – ''Moraxella catarrhalis''<br /> | ||
| + | [[1y9u]], [[2ows]], [[2owt]] – FBP + Fe – ''Bordetella petrussis''<br /> | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D Structures of ferric-binding protein
Updated on 28-February-2023
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
1y4t, 3e13 – FBP + Fe – Campylobacter jejuni
7li0, 7li1 – FBP + Fe – Moraxella catarrhalis
1y9u, 2ows, 2owt – FBP + Fe – Bordetella petrussis
References
- ↑ 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
