1llf
From Proteopedia
(New page: 200px<br /><applet load="1llf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1llf, resolution 1.4Å" /> '''Cholesterol Esterase ...) |
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| - | [[Image:1llf.gif|left|200px]]<br /><applet load="1llf" size=" | + | [[Image:1llf.gif|left|200px]]<br /><applet load="1llf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1llf, resolution 1.4Å" /> | caption="1llf, resolution 1.4Å" /> | ||
'''Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution'''<br /> | '''Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of a Candida cylindracea cholesterol | + | 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== | ==About this Structure== | ||
| - | 1LLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_cylindracea Candida cylindracea] with F23 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http:// | + | 1LLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_cylindracea Candida cylindracea] with <scene name='pdbligand=F23:'>F23</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sterol ester acylhydrolase]] | [[Category: sterol ester acylhydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:01 2008'' |
Revision as of 11:46, 21 February 2008
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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 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
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