2es4
From Proteopedia
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Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase
Overview
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.
About this Structure
2ES4 is a Protein complex structure of sequences from Burkholderia glumae with CA and IOD as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
Structure of a membrane-based steric chaperone in complex with its lipase substrate., Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P, Nat Struct Mol Biol. 2006 Apr;13(4):374-5. Epub 2006 Mar 5. PMID:16518399
Page seeded by OCA on Wed Nov 21 10:06:49 2007
Categories: Burkholderia glumae | Protein complex | Triacylglycerol lipase | Gelder, P.Van. | Pauwels, K. | Savvides, S.N. | Tommassen, J. | Wyns, L. | CA | IOD | A/b hydrolase fold | All alpha helix protein | Extensive interaction area | Protein-protein complex | Steric chaperone | Triacylglycerol hydrolase
