| Title : Structure of a membrane-based steric chaperone in complex with its lipase substrate - Pauwels_2006_Nat.Struct.Mol.Biol_13_374 |
| Author(s) : Pauwels K , Lustig A , Wyns L , Tommassen J , Savvides SN , Van Gelder P |
| Ref : Nat Struct Mol Biol , 13 :374 , 2006 |
|
Abstract :
Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform. |
| PubMedSearch : Pauwels_2006_Nat.Struct.Mol.Biol_13_374 |
| PubMedID: 16518399 |
| Gene_locus related to this paper: burgl-lipas |
| Gene_locus | burgl-lipas |
| Structure | 2ES4 |
Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P (2006)
Structure of a membrane-based steric chaperone in complex with its lipase substrate
Nat Struct Mol Biol
13 :374
Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P (2006)
Nat Struct Mol Biol
13 :374