1LLF

Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution

Summary for 1LLF

• Entry DOI: 10.2210/pdb1llf/pdb
• Related: 1CLE
• Descriptor: Lipase 3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, TRICOSANOIC ACID, ... (4 entities in total)
• Functional Keywords: candida cylindracea cholesterol esterase, sterol ester acylhydrolase, hydrolase
• Biological source: Candida cylindracea
• Total number of polymer chains: 2
• Total formula weight: 117093.81

Authors

Pletnev, V.,Addlagatta, A.,Wawrzak, Z.,Duax, W. (deposition date: 2002-04-28, release date: 2003-01-07, Last modification date: 2023-08-16)

Primary citation

Pletnev, V.,Addlagatta, A.,Wawrzak, Z.,Duax, W.
Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution.
Acta Crystallogr.,Sect.D, 59:50-56, 2003

PubMed Abstract: 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.

PubMed: 12499539
DOI: 10.1107/S0907444902018851

Experimental method

X-RAY DIFFRACTION (1.4 Å)