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1llf
From Proteopedia
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Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution
Overview
The three-dimensional structure of a Candida cylindracea cholesterol, esterase (ChE) homodimer (534 x 2 amino acids) in complex with a ligand of, proposed formula C(23)H(48)O(2) has been determined at 1.4 A resolution in, space group P1 using synchrotron low-temperature data. The structure, refined to R = 0.136 and R(free) = 0.169 and has revealed new, stereochemical details in addition to those detected for the apo- and, holo-forms at 1.9 and 2.0 A resolution, respectively [Ghosh et al. (1995), Structure, 3, 279-288]. The cholesterol esterase structure is a dimer with, four spatially separated interfacial contact areas and two, symmetry-related pairs of openings to an internal intradimer cavity., Hydrophobic active-site gorges in each subunit face each other across a, central interfacial cavity. The ChE subunits have carbohydrate chains, attached to their Asn314 and Asn351 residues, with two ordered, N-acetyl-D-glucosoamine moieties visible at each site. The side chains of, 14 residues have two alternative conformations with occupancy values of, 0.5 +/- 0.2. For each subunit the electron density in the enzyme, active-site gorge is well modeled by a C(23)-chain fatty acid.
About this Structure
1LLF is a Single protein structure of sequence from Candida cylindracea with F23 as ligand. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution., Pletnev V, Addlagatta A, Wawrzak Z, Duax W, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):50-6. Epub 2002 Dec, 19. PMID:12499539
Page seeded by OCA on Tue Nov 20 20:39:14 2007
