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Title

Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements

AuthorsCarrasco-López, César ; Godoy, César A. ; Rivas, Blanca de las ; Fernández-Lorente, Gloria ; Palomo, José Miguel ; Guisán, José Manuel ; Fernández-Lafuente, Roberto ; Martínez-Ripoll, Martín ; Hermoso, Juan A.
KeywordsCrystal structure
Geobacillus thermocatenulatus
Lipase
Issue Date13-Feb-2009
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 284(7): 4365-4372 (2009)
AbstractThe bacterial thermoalkalophilic lipases that hydrolyze saturated fatty acids at 60–75°C and pH 8–10 are grouped as the lipase family I.5. We report here the crystal structure of the lipase from Geobacillus thermocatenulatus, the first structure of a member of the lipase family I.5 showing an open configuration. Unexpectedly, enzyme activation involves large structural rearrangements of around 70 amino acids and the concerted movement of two lids, the α6- and α7-helices, unmasking the active site. Central in the restructuring process of the lids are both the transfer of bulky hydrophobic residues out of the N-terminal end of the α6-helix and the incorporation of short side chain residues to the α6 C-terminal end. All these structural changes are stabilized by the Zn(2+)-binding domain, which is characteristic of this family of lipases. Two detergent molecules are placed in the active site, mimicking chains of the triglyceride substrate, demonstrating the position of the oxyanion hole and the three pockets that accommodate the sn-1, sn-2, and sn-3 fatty acids chains. The combination of structural and biochemical studies indicate that the lid opening is not mediated by temperature but triggered by interaction with lipid substrate.
Description8 pages.-- PMID: 19056729 [PubMed].-- Available online Dec 3, 2008.
Supporting information available at: http://www.jbc.org/cgi/content/full/M808268200/DC1
Publisher version (URL)http://dx.doi.org/10.1074/jbc.M808268200
URIhttp://hdl.handle.net/10261/12503
DOI10.1074/jbc.M808268200
ISSN0021-9258
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