1ji3
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(New page: 200px<br /><applet load="1ji3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ji3, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 21:32, 24 November 2007
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CRYSTAL STRUCTURE OF THE FIRST THERMOSTABLE BACTERIAL LIPASE FROM BACILLUS STEAROTHERMOPHILUS
Overview
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.
About this Structure
1JI3 is a Single protein structure of sequence from Geobacillus stearothermophilus with CA and ZN as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of a thermostable lipase from Bacillus stearothermophilus P1., Tyndall JD, Sinchaikul S, Fothergill-Gilmore LA, Taylor P, Walkinshaw MD, J Mol Biol. 2002 Nov 8;323(5):859-69. PMID:12417199
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