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3bwu
From Proteopedia
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|PDB= 3bwu |SIZE=350|CAPTION= <scene name='initialview01'>3bwu</scene>, resolution 1.760Å | |PDB= 3bwu |SIZE=350|CAPTION= <scene name='initialview01'>3bwu</scene>, resolution 1.760Å | ||
|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Residue+D+126'>AC1</scene>, <scene name='pdbsite=AC2:Edo+Binding+Site+For+Residue+C+206'>AC2</scene>, <scene name='pdbsite=AC3:Edo+Binding+Site+For+Residue+C+207'>AC3</scene>, <scene name='pdbsite=AC4:Edo+Binding+Site+For+Residue+C+208'>AC4</scene>, <scene name='pdbsite=AC5:Edo+Binding+Site+For+Residue+F+5'>AC5</scene>, <scene name='pdbsite=AC6:Edo+Binding+Site+For+Residue+C+209'>AC6</scene>, <scene name='pdbsite=AC7:Edo+Binding+Site+For+Residue+C+210'>AC7</scene>, <scene name='pdbsite=AC8:Edo+Binding+Site+For+Residue+C+211'>AC8</scene>, <scene name='pdbsite=AC9:Edo+Binding+Site+For+Residue+F+9'>AC9</scene>, <scene name='pdbsite=BC1:Edo+Binding+Site+For+Residue+C+212'>BC1</scene>, <scene name='pdbsite=BC2:Edo+Binding+Site+For+Residue+D+127'>BC2</scene>, <scene name='pdbsite=BC3:Edo+Binding+Site+For+Residue+C+213'>BC3</scene>, <scene name='pdbsite=BC4:Edo+Binding+Site+For+Residue+F+155'>BC4</scene> and <scene name='pdbsite=BC5:Peg+Binding+Site+For+Residue+C+214'>BC5</scene> | |SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Residue+D+126'>AC1</scene>, <scene name='pdbsite=AC2:Edo+Binding+Site+For+Residue+C+206'>AC2</scene>, <scene name='pdbsite=AC3:Edo+Binding+Site+For+Residue+C+207'>AC3</scene>, <scene name='pdbsite=AC4:Edo+Binding+Site+For+Residue+C+208'>AC4</scene>, <scene name='pdbsite=AC5:Edo+Binding+Site+For+Residue+F+5'>AC5</scene>, <scene name='pdbsite=AC6:Edo+Binding+Site+For+Residue+C+209'>AC6</scene>, <scene name='pdbsite=AC7:Edo+Binding+Site+For+Residue+C+210'>AC7</scene>, <scene name='pdbsite=AC8:Edo+Binding+Site+For+Residue+C+211'>AC8</scene>, <scene name='pdbsite=AC9:Edo+Binding+Site+For+Residue+F+9'>AC9</scene>, <scene name='pdbsite=BC1:Edo+Binding+Site+For+Residue+C+212'>BC1</scene>, <scene name='pdbsite=BC2:Edo+Binding+Site+For+Residue+D+127'>BC2</scene>, <scene name='pdbsite=BC3:Edo+Binding+Site+For+Residue+C+213'>BC3</scene>, <scene name='pdbsite=BC4:Edo+Binding+Site+For+Residue+F+155'>BC4</scene> and <scene name='pdbsite=BC5:Peg+Binding+Site+For+Residue+C+214'>BC5</scene> | ||
| - | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= fimC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), fimD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), fimF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= fimC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), fimD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), fimF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ze3|1ZE3]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwu OCA], [http://www.ebi.ac.uk/pdbsum/3bwu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bwu RCSB]</span> | ||
}} | }} | ||
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[[Category: Eidam, O.]] | [[Category: Eidam, O.]] | ||
[[Category: Grutter, M G.]] | [[Category: Grutter, M G.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: PEG]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
[[Category: mebrane protein]] | [[Category: mebrane protein]] | ||
| Line 36: | Line 37: | ||
[[Category: usher]] | [[Category: usher]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:29:25 2008'' |
Revision as of 02:29, 31 March 2008
| |||||||
| , resolution 1.760Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , and | ||||||
| Ligands: | , | ||||||
| Gene: | fimC (Escherichia coli), fimD (Escherichia coli), fimF (Escherichia coli) | ||||||
| Related: | 1ZE3
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)
Overview
Type 1 pili, anchored to the outer membrane protein FimD, enable uropathogenic Escherichia coli to attach to host cells. During pilus biogenesis, the N-terminal periplasmic domain of FimD (FimD(N)) binds complexes between the chaperone FimC and pilus subunits via its partly disordered N-terminal segment, as recently shown for the FimC-FimH(P)-FimD(N) ternary complex. We report the structure of a new ternary complex (FimC-FimF(t)-FimD(N)) with the subunit FimF(t) instead of FimH(p). FimD(N) recognizes FimC-FimF(t) and FimC-FimH(P) very similarly, predominantly through hydrophobic interactions. The conserved binding mode at a "hot spot" on the chaperone surface could guide the design of pilus assembly inhibitors.
About this Structure
3BWU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD., Eidam O, Dworkowski FS, Glockshuber R, Grutter MG, Capitani G, FEBS Lett. 2008 Mar 5;582(5):651-5. Epub 2008 Jan 31. PMID:18242189
Page seeded by OCA on Mon Mar 31 05:29:25 2008
