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2es4
From Proteopedia
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | lifO, lipB (Burkholderia glumae) | ||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 16:43:51 2008
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
