6A12
X-ray structure of lipase from Geobacillus thermoleovorans
Summary for 6A12
| Entry DOI | 10.2210/pdb6a12/pdb |
| Descriptor | Lipase, CALCIUM ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | lipase, geobacillus thermoleovorans, hydrolase |
| Biological source | Geobacillus thermoleovorans (Bacillus thermoleovorans) |
| Total number of polymer chains | 1 |
| Total formula weight | 43433.80 |
| Authors | Moharana, T.R.,Pal, B.,Rao, N.M. (deposition date: 2018-06-06, release date: 2018-06-20, Last modification date: 2023-11-22) |
| Primary citation | Moharana, T.R.,Pal, B.,Rao, N.M. X-ray structure and characterization of a thermostable lipase from Geobacillus thermoleovorans. Biochem. Biophys. Res. Commun., 508:145-151, 2019 Cited by PubMed Abstract: Thermo-alkalophilic bacterium, Geobacillus thermoleovorans secrets many enzymes including a 43 kDa extracellular lipase. Significant thermostability, organic solvent stability and wide substrate preferences for hydrolysis drew our attention to solve its structure by crystallography. The structure was solved by molecular replacement method and refined up to 2.14 Å resolution. Structure of the lipase showed an alpha-beta fold with 19 α-helices and 10 β-sheets. The active site remains covered by a lid. One calcium and one zinc atom was found in the crystal. The structure showed a major difference (rmsd 5.6 Å) from its closest homolog in the amino acid region 191 to 203. Thermal unfolding of the lipase showed that the lipase is highly stable with T of 76 °C. C NMR spectra of products upon triglyceride hydrolysate revealed that the lipase hydrolyses at both sn-1 and sn-2 positions with equal efficiency. PubMed: 30471860DOI: 10.1016/j.bbrc.2018.11.105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.145 Å) |
Structure validation
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