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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
caption="1llf, resolution 1.4&Aring;" />
'''Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution'''<br />


==Overview==
==Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution==
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.
<StructureSection load='1llf' size='340' side='right'caption='[[1llf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1llf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Limtongozyma_cylindracea Limtongozyma cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F23:TRICOSANOIC+ACID'>F23</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1llf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llf OCA], [https://pdbe.org/1llf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llf RCSB], [https://www.ebi.ac.uk/pdbsum/1llf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6S5M9_9ASCO Q6S5M9_9ASCO]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1llf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1llf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:12499539</ref>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LLF OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12499539 12499539]
</div>
[[Category: Candida cylindracea]]
<div class="pdbe-citations 1llf" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Triacylglycerol lipase]]
[[Category: Addlagatta, A.]]
[[Category: Duax, W.]]
[[Category: Pletnev, V.]]
[[Category: Wawrzak, Z.]]
[[Category: F23]]
[[Category: candida cylindracea cholesterol esterase]]
[[Category: crystal structure]]
[[Category: sterol ester acylhydrolase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:39:14 2007''
==See Also==
*[[Cholesterol esterase|Cholesterol esterase]]
*[[Cholesterol esterase 3D structures|Cholesterol esterase 3D structures]]
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Limtongozyma cylindracea]]
[[Category: Addlagatta A]]
[[Category: Duax W]]
[[Category: Pletnev V]]
[[Category: Wawrzak Z]]
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