1ORJ

FLAGELLAR EXPORT CHAPERONE

Summary for 1ORJ

• Entry DOI: 10.2210/pdb1orj/pdb
• Related: 1ORY
• Descriptor: flagellar protein FliS (2 entities in total)
• Functional Keywords: flagellin, flagellar export, chaperone, flagellum, four helix bundle
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 4
• Total formula weight: 62151.66

Authors

Evdokimov, A.G.,Phan, J.,Tropea, J.E.,Routzahn, K.M.,Peters III, H.K.,Pokross, M.,Waugh, D.S. (deposition date: 2003-03-13, release date: 2003-09-16, Last modification date: 2024-02-14)

Primary citation

Evdokimov, A.G.,Phan, J.,Tropea, J.E.,Routzahn, K.M.,Peters III, H.K.,Pokross, M.,Waugh, D.S.
Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion
Nat.Struct.Biol., 10:789-793, 2003

PubMed Abstract: 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.

PubMed: 12958592
DOI: 10.1038/nsb982

Experimental method

X-RAY DIFFRACTION (2.25 Å)