2QUB
Crystal structure of extracellular lipase LipA from Serratia marcescens
Summary for 2QUB
| Entry DOI | 10.2210/pdb2qub/pdb |
| Related | 2QUA |
| Descriptor | Extracellular lipase, CALCIUM ION (3 entities in total) |
| Functional Keywords | beta roll, alpha/beta hydrolase, helical hairpin, hydrolase |
| Biological source | Serratia marcescens |
| Total number of polymer chains | 6 |
| Total formula weight | 392354.55 |
| Authors | Meier, R.,Baumann, U. (deposition date: 2007-08-04, release date: 2007-08-28, Last modification date: 2024-02-21) |
| Primary citation | Meier, R.,Drepper, T.,Svensson, V.,Jaeger, K.E.,Baumann, U. A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens. J.Biol.Chem., 282:31477-31483, 2007 Cited by PubMed Abstract: 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-A 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 alpha/beta hydrolase fold in an open conformation, where the putative lid helix is anchored by a Ca(2+) 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 beta-roll domains that pack tightly against each other. Variations of the consensus sequence of the tandem repeats within the second beta-roll result in an asymmetric Ca(2+) binding on only one side of the roll. The analysis of the properties of the beta-roll domains suggests an intramolecular chaperone function. PubMed: 17728256DOI: 10.1074/jbc.M704942200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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