1gz7
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CRYSTAL STRUCTURE OF THE CLOSED STATE OF LIPASE 2 FROM CANDIDA RUGOSA
OverviewOverview
The yeast Candida rugosa produces several closely related extracellular, lipases that differ in their substrate specificity. Here, we report the, crystal structure of the isoenzyme lipase 2 at 1.97A resolution in its, closed conformation. Lipase 2 shows a 79.4% amino acid sequence identity, with lipase 1 and 82.2% with lipase 3, which makes it relevant to compare, these three isoenzymes. Despite this high level of sequence identity, structural comparisons reveal several amino acid changes affecting the, flap (residue 69), the substrate-binding pocket (residues 127, 132 and, 450) and the mouth of the hydrophobic tunnel (residues 296 and 344), which, may be responsible for the different substrate specificity and catalytic, properties of this group of enzymes. Also, these comparisons reveal ... [(full description)]
About this StructureAbout this Structure
1GZ7 is a [Single protein] structure of sequence from [Candida rugosa] with GOL as [ligand]. Active as [Triacylglycerol lipase], with EC number [3.1.1.3]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97A resolution., Mancheno JM, Pernas MA, Martinez MJ, Ochoa B, Rua ML, Hermoso JA, J Mol Biol. 2003 Oct 3;332(5):1059-69. PMID:14499609
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