1CLE

STRUCTURE OF UNCOMPLEXED AND LINOLEATE-BOUND CANDIDA CYLINDRACEA CHOLESTEROL ESTERASE

Summary for 1CLE

• Entry DOI: 10.2210/pdb1cle/pdb
• Descriptor: CHOLESTEROL ESTERASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: esterase, substrate/product-bound, lipase
• Biological source: Candida cylindracea
• Total number of polymer chains: 2
• Total formula weight: 117438.27

Authors

Ghosh, D. (deposition date: 1995-02-08, release date: 1996-03-08, Last modification date: 2024-10-23)

Primary citation

Ghosh, D.,Wawrzak, Z.,Pletnev, V.Z.,Li, N.,Kaiser, R.,Pangborn, W.,Jornvall, H.,Erman, M.,Duax, W.L.
Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase.
Structure, 3:279-288, 1995

PubMed Abstract: Candida cylindracea cholesterol esterase (CE) reversibly hydrolyzes cholesteryl linoleate and oleate. CE belongs to the same alpha/beta hydrolase superfamily as triacylglycerol acyl hydrolases and cholinesterases. Other members of the family that have been studied by X-ray crystallography include Torpedo californica acetylcholinesterase, Geotrichum candidum lipase and Candida rugosa lipase. CE is homologous to C. rugosa lipase 1, a triacylglycerol acyl hydrolase, with which it shares 89% sequence identity. The present study explores the details of dimer formation of CE and the basis for its substrate specificity.

PubMed: 7788294
DOI: 10.1016/S0969-2126(01)00158-7

Experimental method

X-RAY DIFFRACTION (2 Å)