1orj: Difference between revisions
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'''FLAGELLAR EXPORT CHAPERONE''' | '''FLAGELLAR EXPORT CHAPERONE''' | ||
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[[Category: Tropea, J E.]] | [[Category: Tropea, J E.]] | ||
[[Category: Waugh, D S.]] | [[Category: Waugh, D S.]] | ||
[[Category: | [[Category: Chaperone]] | ||
[[Category: | [[Category: Flagellar export]] | ||
[[Category: | [[Category: Flagellin]] | ||
[[Category: | [[Category: Flagellum]] | ||
[[Category: | [[Category: Four helix bundle]] | ||
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Revision as of 04:11, 3 May 2008
FLAGELLAR EXPORT CHAPERONE
OverviewOverview
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 StructureAbout this Structure
1ORJ is a Single protein structure of sequence from Aquifex aeolicus vf5. Full crystallographic information is available from OCA.
ReferenceReference
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 04:11:44 2008