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| | ==Crystal structure of the FimD translocation domain== | | ==Crystal structure of the FimD translocation domain== |
| - | <StructureSection load='3ohn' size='340' side='right' caption='[[3ohn]], [[Resolution|resolution]] 3.01Å' scene=''> | + | <StructureSection load='3ohn' size='340' side='right'caption='[[3ohn]], [[Resolution|resolution]] 3.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ohn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OHN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ohn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OHN FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rfz|3rfz]]</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]] 3.011Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3ohn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ohn OCA], [https://pdbe.org/3ohn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ohn RCSB], [https://www.ebi.ac.uk/pdbsum/3ohn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ohn ProSAT]</span></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=3ohn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ohn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ohn RCSB], [http://www.ebi.ac.uk/pdbsum/3ohn PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FIMD_ECOLI FIMD_ECOLI] Involved in the export and assembly of FimA fimbrial subunits across the outer membrane. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3ohn" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Li, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Wang, T]] | + | [[Category: Li H]] |
| - | [[Category: Beta-barrel]] | + | [[Category: Wang T]] |
| - | [[Category: Membrane protein]]
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| - | [[Category: Outer membrane]]
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| - | [[Category: Protein translocation]]
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| Structural highlights
Function
FIMD_ECOLI Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
Publication Abstract from PubMed
Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length FimD usher bound to the FimC-FimH chaperone-adhesin complex and that of the unbound form of the FimD translocation domain. The FimD-FimC-FimH structure shows FimH inserted inside the FimD 24-stranded beta-barrel translocation channel. FimC-FimH is held in place through interactions with the two carboxy-terminal periplasmic domains of FimD, a binding mode confirmed in solution by electron paramagnetic resonance spectroscopy. To accommodate FimH, the usher plug domain is displaced from the barrel lumen to the periplasm, concomitant with a marked conformational change in the beta-barrel. The amino-terminal domain of FimD is observed in an ideal position to catalyse incorporation of a newly recruited chaperone-subunit complex. The FimD-FimC-FimH structure provides unique insights into the pilus subunit incorporation cycle, and captures the first view of a protein transporter in the act of secreting its cognate substrate.
Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate.,Phan G, Remaut H, Wang T, Allen WJ, Pirker KF, Lebedev A, Henderson NS, Geibel S, Volkan E, Yan J, Kunze MB, Pinkner JS, Ford B, Kay CW, Li H, Hultgren SJ, Thanassi DG, Waksman G Nature. 2011 Jun 2;474(7349):49-53. PMID:21637253[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Phan G, Remaut H, Wang T, Allen WJ, Pirker KF, Lebedev A, Henderson NS, Geibel S, Volkan E, Yan J, Kunze MB, Pinkner JS, Ford B, Kay CW, Li H, Hultgren SJ, Thanassi DG, Waksman G. Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature. 2011 Jun 2;474(7349):49-53. PMID:21637253 doi:10.1038/nature10109
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