1ory

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[[Image:1ory.gif|left|200px]]
[[Image:1ory.gif|left|200px]]
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{{Structure
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|PDB= 1ory |SIZE=350|CAPTION= <scene name='initialview01'>1ory</scene>, resolution 2.45&Aring;
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The line below this paragraph, containing "STRUCTURE_1ory", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|GENE= FliS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 Aquifex aeolicus VF5]), FLAA OR FLIC OR AQ_1998 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus])
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|DOMAIN=
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{{STRUCTURE_1ory| PDB=1ory | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ory FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ory OCA], [http://www.ebi.ac.uk/pdbsum/1ory PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ory RCSB]</span>
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'''FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER'''
'''FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER'''
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[[Category: Tropea, J E.]]
[[Category: Tropea, J E.]]
[[Category: Waugh, D S.]]
[[Category: Waugh, D S.]]
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[[Category: cytosolic export chaperone]]
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[[Category: Cytosolic export chaperone]]
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[[Category: flagellar chaperone]]
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[[Category: Flagellar chaperone]]
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[[Category: flagellin]]
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[[Category: Flagellin]]
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[[Category: flic]]
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[[Category: Flic]]
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[[Category: fli]]
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[[Category: Fli]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:12:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:49:31 2008''
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Revision as of 01:12, 3 May 2008

Image:1ory.gif

Template:STRUCTURE 1ory

FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER


Overview

Assembly of the bacterial flagellum and type III secretion in pathogenic bacteria require cytosolic export chaperones that interact with mobile components to facilitate their secretion. Although their amino acid sequences are not conserved, the structures of several type III secretion chaperones revealed striking similarities between their folds and modes of substrate recognition. Here, we report the first crystallographic structure of a flagellar export chaperone, Aquifex aeolicus FliS. FliS adopts a novel fold that is clearly distinct from those of the type III secretion chaperones, indicating that they do not share a common evolutionary origin. However, the structure of FliS in complex with a fragment of FliC (flagellin) reveals that, like the type III secretion chaperones, flagellar export chaperones bind their target proteins in extended conformation and suggests that this mode of recognition may be widely used in bacteria.

About this Structure

1ORY is a Protein complex structure of sequences from Aquifex aeolicus and Aquifex aeolicus vf5. Full crystallographic information is available from OCA.

Reference

Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion., Evdokimov AG, Phan J, Tropea JE, Routzahn KM, Peters HK, Pokross M, Waugh DS, Nat Struct Biol. 2003 Oct;10(10):789-93. Epub 2003 Sep 7. PMID:12958592 Page seeded by OCA on Sat May 3 04:12:34 2008

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