|
|
Line 3: |
Line 3: |
| <StructureSection load='6bpo' size='340' side='right'caption='[[6bpo]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='6bpo' size='340' side='right'caption='[[6bpo]], [[Resolution|resolution]] 2.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6bpo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BPO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bpo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BPO FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fiu, ybiL, b0805, JW0790 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bpo OCA], [http://pdbe.org/6bpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bpo RCSB], [http://www.ebi.ac.uk/pdbsum/6bpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bpo ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bpo OCA], [https://pdbe.org/6bpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bpo RCSB], [https://www.ebi.ac.uk/pdbsum/6bpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bpo ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/FIU_ECOLI FIU_ECOLI]] Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492.<ref>PMID:12949180</ref> <ref>PMID:16718603</ref> <ref>PMID:2139424</ref> <ref>PMID:2407721</ref> <ref>PMID:3072926</ref> | + | [https://www.uniprot.org/uniprot/FIU_ECOLI FIU_ECOLI] Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492.<ref>PMID:12949180</ref> <ref>PMID:16718603</ref> <ref>PMID:2139424</ref> <ref>PMID:2407721</ref> <ref>PMID:3072926</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
Line 23: |
Line 23: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Grinter, R]] | + | [[Category: Grinter R]] |
- | [[Category: Antibiotic uptake]]
| + | |
- | [[Category: Ferric-catecholate]]
| + | |
- | [[Category: Iron transporter]]
| + | |
- | [[Category: Membrane protein]]
| + | |
- | [[Category: Membrane transport]]
| + | |
- | [[Category: Tonb-dependent receptor]]
| + | |
| Structural highlights
Function
FIU_ECOLI Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
The ferric iron uptake (Fiu) transporter from Escherichia coli functions in the transport of iron-catecholate complexes across the bacterial outer membrane, providing the bacterium with iron, which is essential for growth. Recently, it has become clear that Fiu also represents a liability for E. coli because its activity allows the import of antimicrobial compounds that mimic catecholate. This inadvertent import suggests the potential utility of antimicrobial catechol-siderophore mimetics in managing bacterial infections. However, in order to fully exploit these compounds, a detailed understanding of the mechanism of transport through Fiu and related transporters is required. To address this question, we determined the crystal structure of Fiu at 2.1-2.9 A and analyzed its function in E. coli. Through analysis of the Fiu crystal structure, in combination with in silico docking and mutagenesis, we provide insight into how Fiu and related transporters bind catecholate in a surface-exposed cavity. Moreover, through the determination of the structure of Fiu in multiple crystal states, we revealed the presence of a large, selectively-gated cavity in the interior of this transporter. This chamber is large enough to accommodate the Fiu substrate and may allow for the import of substrates via a two-step mechanism. This would avoid channel formation through the transporter and the inadvertent import of toxic molecules. As Fiu and its homologs are the targets of substrate-mimicking antibiotics, these results may assist in the development of these compounds.
The structure of the bacterial iron-catecholate transporter Fiu suggests that it imports substrates via a two-step mechanism.,Grinter R, Lithgow T J Biol Chem. 2019 Nov 11. pii: RA119.011018. doi: 10.1074/jbc.RA119.011018. PMID:31712312[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Patzer SI, Baquero MR, Bravo D, Moreno F, Hantke K. The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN. Microbiology. 2003 Sep;149(Pt 9):2557-70. doi: 10.1099/mic.0.26396-0. PMID:12949180 doi:http://dx.doi.org/10.1099/mic.0.26396-0
- ↑ Destoumieux-Garzon D, Peduzzi J, Thomas X, Djediat C, Rebuffat S. Parasitism of iron-siderophore receptors of Escherichia coli by the siderophore-peptide microcin E492m and its unmodified counterpart. Biometals. 2006 Apr;19(2):181-91. doi: 10.1007/s10534-005-4452-9. PMID:16718603 doi:http://dx.doi.org/10.1007/s10534-005-4452-9
- ↑ Hantke K. Dihydroxybenzoylserine--a siderophore for E. coli. FEMS Microbiol Lett. 1990 Jan 15;55(1-2):5-8. PMID:2139424
- ↑ Nikaido H, Rosenberg EY. Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechols: study with beta-lactam antibiotics containing catechol and analogous groups. J Bacteriol. 1990 Mar;172(3):1361-7. PMID:2407721
- ↑ Curtis NA, Eisenstadt RL, East SJ, Cornford RJ, Walker LA, White AJ. Iron-regulated outer membrane proteins of Escherichia coli K-12 and mechanism of action of catechol-substituted cephalosporins. Antimicrob Agents Chemother. 1988 Dec;32(12):1879-86. PMID:3072926
- ↑ Grinter R, Lithgow T. The structure of the bacterial iron-catecholate transporter Fiu suggests that it imports substrates via a two-step mechanism. J Biol Chem. 2019 Nov 11. pii: RA119.011018. doi: 10.1074/jbc.RA119.011018. PMID:31712312 doi:http://dx.doi.org/10.1074/jbc.RA119.011018
|