1ze3

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[[Image:1ze3.gif|left|200px]]<br /><applet load="1ze3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ze3.gif|left|200px]]
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caption="1ze3, resolution 1.84&Aring;" />
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'''Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH'''<br />
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{{Structure
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|PDB= 1ze3 |SIZE=350|CAPTION= <scene name='initialview01'>1ze3</scene>, resolution 1.84&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY=
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|GENE= fimC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), fimH ([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])
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}}
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'''Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZE3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZE3 OCA].
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1ZE3 is a [[Protein complex]] structure of sequences 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=1ZE3 OCA].
==Reference==
==Reference==
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Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD., Nishiyama M, Horst R, Eidam O, Herrmann T, Ignatov O, Vetsch M, Bettendorff P, Jelesarov I, Grutter MG, Wuthrich K, Glockshuber R, Capitani G, EMBO J. 2005 Jun 15;24(12):2075-86. Epub 2005 May 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15920478 15920478]
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Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD., Nishiyama M, Horst R, Eidam O, Herrmann T, Ignatov O, Vetsch M, Bettendorff P, Jelesarov I, Grutter MG, Wuthrich K, Glockshuber R, Capitani G, EMBO J. 2005 Jun 15;24(12):2075-86. Epub 2005 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15920478 15920478]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: usher]]
[[Category: usher]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:22 2008''

Revision as of 13:34, 20 March 2008

Image:1ze3.gif


PDB ID 1ze3

Drag the structure with the mouse to rotate
, resolution 1.84Å
Ligands:
Gene: fimC (Escherichia coli), fimH (Escherichia coli), fimD (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH


Overview

Adhesive type 1 pili from uropathogenic Escherichia coli are filamentous protein complexes that are attached to the assembly platform FimD in the outer membrane. During pilus assembly, FimD binds complexes between the chaperone FimC and type 1 pilus subunits in the periplasm and mediates subunit translocation to the cell surface. Here we report nuclear magnetic resonance and X-ray protein structures of the N-terminal substrate recognition domain of FimD (FimD(N)) before and after binding of a chaperone-subunit complex. FimD(N) consists of a flexible N-terminal segment of 24 residues, a structured core with a novel fold, and a C-terminal hinge segment. In the ternary complex, residues 1-24 of FimD(N) specifically interact with both FimC and the subunit, acting as a sensor for loaded FimC molecules. Together with in vivo complementation studies, we show how this mechanism enables recognition and discrimination of different chaperone-subunit complexes by bacterial pilus assembly platforms.

About this Structure

1ZE3 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD., Nishiyama M, Horst R, Eidam O, Herrmann T, Ignatov O, Vetsch M, Bettendorff P, Jelesarov I, Grutter MG, Wuthrich K, Glockshuber R, Capitani G, EMBO J. 2005 Jun 15;24(12):2075-86. Epub 2005 May 26. PMID:15920478

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