1JI3

CRYSTAL STRUCTURE OF THE FIRST THERMOSTABLE BACTERIAL LIPASE FROM BACILLUS STEAROTHERMOPHILUS

Summary for 1JI3

• Entry DOI: 10.2210/pdb1ji3/pdb
• Related: 1cvl 4lip
• Descriptor: lipase, CALCIUM ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: lipase, metal-binding, thermophilic, hydrolase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 2
• Total formula weight: 86831.46

Authors

Tyndall, J.D.A.,Sinchaikul, S.,Fothergill-Gilmore, L.A.,Taylor, P.,Walkinshaw, M.D. (deposition date: 2001-06-29, release date: 2002-11-01, Last modification date: 2024-02-07)

Primary citation

Tyndall, J.D.A.,Sinchaikul, S.,Fothergill-Gilmore, L.A.,Taylor, P.,Walkinshaw, M.D.
Crystal Structure of a Thermostable Lipase from Bacillus stearothermophilus P1
J.Mol.Biol., 323:859-869, 2002

PubMed Abstract: We describe the first lipase structure from a thermophilic organism. It shares less than 20% amino acid sequence identity with other lipases for which there are crystal structures, and shows significant insertions compared with the typical alpha/beta hydrolase canonical fold. The structure contains a zinc-binding site which is unique among all lipases with known structures, and which may play a role in enhancing thermal stability. Zinc binding is mediated by two histidine and two aspartic acid residues. These residues are present in comparable positions in the sequences of certain lipases for which there is as yet no crystal structural information, such as those from Staphylococcal species and Arabidopsis thaliana. The structure of Bacillus stearothermophilus P1 lipase provides a template for other thermostable lipases, and offers insight into mechanisms used to enhance thermal stability which may be of commercial value in engineering lipases for industrial uses.

PubMed: 12417199
DOI: 10.1016/S0022-2836(02)01004-5

Experimental method

X-RAY DIFFRACTION (2.2 Å)