1ory

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[[Image:1ory.gif|left|200px]]<br /><applet load="1ory" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ory.gif|left|200px]]
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caption="1ory, resolution 2.45&Aring;" />
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'''FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER'''<br />
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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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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|ACTIVITY=
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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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}}
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'''FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ORY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [http://en.wikipedia.org/wiki/Aquifex_aeolicus_vf5 Aquifex aeolicus vf5] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORY OCA].
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1ORY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [http://en.wikipedia.org/wiki/Aquifex_aeolicus_vf5 Aquifex aeolicus vf5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORY OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12958592 12958592]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12958592 12958592]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus vf5]]
[[Category: Aquifex aeolicus vf5]]
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[[Category: flagellin]]
[[Category: flagellin]]
[[Category: flic]]
[[Category: flic]]
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[[Category: flis]]
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[[Category: fli]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:14:50 2008''

Revision as of 11:14, 20 March 2008

Image:1ory.gif


PDB ID 1ory

Drag the structure with the mouse to rotate
, resolution 2.45Å
Ligands:
Gene: FliS (Aquifex aeolicus VF5), FLAA OR FLIC OR AQ_1998 (Aquifex aeolicus)
Coordinates: save as pdb, mmCIF, xml



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

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