1ory
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ory" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ory, resolution 2.45Å" /> '''FLAGELLAR EXPORT CHA...)
Next diff →
Revision as of 21:01, 20 November 2007
|
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 with PO4 as ligand. 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 Tue Nov 20 23:08:40 2007
