1ze3
From Proteopedia
(New page: 200px<br /><applet load="1ze3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ze3, resolution 1.84Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ze3.gif|left|200px]]<br /><applet load="1ze3" size=" | + | [[Image:1ze3.gif|left|200px]]<br /><applet load="1ze3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ze3, resolution 1.84Å" /> | caption="1ze3, resolution 1.84Å" /> | ||
'''Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH'''<br /> | '''Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Adhesive type 1 pili from uropathogenic Escherichia coli are filamentous | + | 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== | ==About this Structure== | ||
| - | 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 EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Eidam, O.]] | [[Category: Eidam, O.]] | ||
[[Category: Glockshuber, R.]] | [[Category: Glockshuber, R.]] | ||
| - | [[Category: Grutter, M | + | [[Category: Grutter, M G.]] |
[[Category: Herrmann, T.]] | [[Category: Herrmann, T.]] | ||
[[Category: Horst, R.]] | [[Category: Horst, R.]] | ||
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[[Category: usher]] | [[Category: usher]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:43 2008'' |
Revision as of 14:14, 21 February 2008
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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 with as ligand. 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
Page seeded by OCA on Thu Feb 21 16:14:43 2008
Categories: Escherichia coli | Protein complex | Bettendorff, P. | Capitani, G. | Eidam, O. | Glockshuber, R. | Grutter, M G. | Herrmann, T. | Horst, R. | Ignatov, O. | Jelesarov, I. | Nishiyama, M. | Vetsch, M. | Wuthrich, K. | EDO | Soluble domain | Ternary complex with chaperone and pilus subunit | Usher
