3LIP
OPEN CONFORMATION OF PSEUDOMONAS CEPACIA LIPASE
Summary for 3LIP
| Entry DOI | 10.2210/pdb3lip/pdb |
| Descriptor | TRIACYL-GLYCEROL-HYDROLASE, CALCIUM ION (3 entities in total) |
| Functional Keywords | hydrolase, lipase, pseudomonadaceae, catalytic triad, oxyanion, open, without inhibitor |
| Biological source | Burkholderia cepacia |
| Total number of polymer chains | 1 |
| Total formula weight | 33190.84 |
| Authors | Lang, D.A.,Schomburg, D. (deposition date: 1997-04-18, release date: 1997-06-16, Last modification date: 2024-10-09) |
| Primary citation | Schrag, J.D.,Li, Y.,Cygler, M.,Lang, D.,Burgdorf, T.,Hecht, H.J.,Schmid, R.,Schomburg, D.,Rydel, T.J.,Oliver, J.D.,Strickland, L.C.,Dunaway, C.M.,Larson, S.B.,Day, J.,McPherson, A. The open conformation of a Pseudomonas lipase. Structure, 5:187-202, 1997 Cited by PubMed Abstract: . The interfacial activation of lipases results primarily from conformational changes in the enzymes which expose the active site and provide a hydrophobic surface for interaction with the lipid substrate. Comparison of the crystallization conditions used and the structures observed for a variety of lipases suggests that the enzyme conformation is dependent on solution conditions. Pseudomonas cepacia lipase (PCL) was crystallized in conditions from which the open, active conformation of the enzyme was expected. Its three-dimensional structure was determined independently in three different laboratories and was compared with the previously reported closed conformations of the closely related lipases from Pseudomonas glumae (PGL) and Chromobacterium viscosum (CVL). These structures provide new insights into the function of this commercially important family of lipases. PubMed: 9032074DOI: 10.1016/S0969-2126(97)00178-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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