1EX9

CRYSTAL STRUCTURE OF THE PSEUDOMONAS AERUGINOSA LIPASE COMPLEXED WITH RC-(RP,SP)-1,2-DIOCTYLCARBAMOYL-GLYCERO-3-O-OCTYLPHOSPHONATE

Summary for 1EX9

• Entry DOI: 10.2210/pdb1ex9/pdb
• Descriptor: LACTONIZING LIPASE, CALCIUM ION, OCTYL-PHOSPHINIC ACID 1,2-BIS-OCTYLCARBAMOYLOXY-ETHYL ESTER, ... (4 entities in total)
• Functional Keywords: lipase, alpha-beta hydrolase fold, pseudomonas, phosphonate inhibitor, hydrolase
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cell surface: P26876
• Total number of polymer chains: 1
• Total formula weight: 30779.36

Authors

Nardini, M.,Lang, D.A.,Liebeton, K.,Jaeger, K.-E.,Dijkstra, B.W. (deposition date: 2000-05-02, release date: 2000-10-18, Last modification date: 2024-10-09)

Primary citation

Nardini, M.,Lang, D.A.,Liebeton, K.,Jaeger, K.E.,Dijkstra, B.W.
Crystal structure of pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases.
J.Biol.Chem., 275:31219-31225, 2000

PubMed Abstract: The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 A resolution. It is the first structure of a member of homology family I.1 of bacterial lipases. The structure shows a variant of the alpha/beta hydrolase fold, with Ser(82), Asp(229), and His(251) as the catalytic triad residues. Compared with the "canonical" alpha/beta hydrolase fold, the first two beta-strands and one alpha-helix (alphaE) are not present. The absence of helix alphaE allows the formation of a stabilizing intramolecular disulfide bridge. The loop containing His(251) is stabilized by an octahedrally coordinated calcium ion. On top of the active site a lid subdomain is in an open conformation, making the catalytic cleft accessible from the solvent region. A triacylglycerol analogue is covalently bound to Ser(82) in the active site, demonstrating the position of the oxyanion hole and of the three pockets that accommodate the sn-1, sn-2, and sn-3 fatty acid chains. The inhibited enzyme can be thought to mimic the structure of the tetrahedral intermediate that occurs during the acylation step of the reaction. Analysis of the binding mode of the inhibitor suggests that the size of the acyl pocket and the size and interactions of the sn-2 binding pocket are the predominant determinants of the regio- and enantio-preference of the enzyme.

PubMed: 10893416
DOI: 10.1074/jbc.M003903200

Experimental method

X-RAY DIFFRACTION (2.54 Å)