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J. Biol. Chem., Vol. 282, Issue 43, 31477-31483, October 26, 2007

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A Calcium-gated Lid and a Large -Roll Sandwich Are Revealed by the Crystal Structure of Extracellular Lipase from Serratia marcescens^*

Reto Meier, Thomas Drepper, Vera Svensson, Karl-Erich Jaeger¹, and Ulrich Baumann²

From the Department of Chemistry and Biochemistry, University Bern Freiestrasse 3, CH-3012 Bern, Switzerland and Institute of Molecular Enzyme Technology, Heinrich-Heine-University Duesseldorf, Research Centre Juelich, D-52426 Jülich, Germany

Lipase LipA from Serratia marcescens is a 613-amino acid enzyme belonging to family I.3 of lipolytic enzymes that has an important biotechnological application in the production of a chiral precursor for the coronary vasodilator diltiazem. Like other family I.3 lipases, LipA is secreted by Gram-negative bacteria via a type I secretion system and possesses 13 copies of a calcium binding tandem repeat motif, GGXGXDXUX (U, hydrophobic amino acids), in the C-terminal part of the polypeptide chain. The 1.8-Å crystal structure of LipA reveals a close relation to eukaryotic lipases, whereas family I.1 and I.2 enzymes appear to be more distantly related. Interestingly, the structure shows for the N-terminal lipase domain a variation on the canonical / hydrolase fold in an open conformation, where the putative lid helix is anchored by a Ca²⁺ ion essential for activity. Another novel feature observed in this lipase structure is the presence of a helical hairpin additional to the putative lid helix that exposes a hydrophobic surface to the aqueous medium and might function as an additional lid. The tandem repeats form two separated parallel -roll domains that pack tightly against each other. Variations of the consensus sequence of the tandem repeats within the second -roll result in an asymmetric Ca²⁺ binding on only one side of the roll. The analysis of the properties of the -roll domains suggests an intramolecular chaperone function.

Received for publication, June 15, 2007 , and in revised form, July 20, 2007.

The atomic coordinates and structure factors (code 2QUA and 2QUB) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work has been supported by the Swiss National Science Foundation and by the Hochschulstiftung der Universität Bern. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental material.

¹ To whom correspondence may be addressed. Tel.: 49-2461-613716; Fax: 49-2461-612490; E-mail: karl-erich.jaeger{at}fz-juelich.de. ² To whom correspondence may be addressed. Tel.: 41-31-631-4320; Fax: 41-31-6314887; E-mail: ulrich.baumann{at}ibc.unibe.ch.

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