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< | ==Structural and Functional Analysis of a Hormone-Sensitive Lipase like EstE5 from a Metagenome Library== | ||
<StructureSection load='3fak' size='340' side='right'caption='[[3fak]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fak]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FAK 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]] 1.9Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=3fak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fak OCA], [https://pdbe.org/3fak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fak RCSB], [https://www.ebi.ac.uk/pdbsum/3fak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fak ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0GMU2_9BACT Q0GMU2_9BACT] | |||
== 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/fa/3fak_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=3fak ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hormone-sensitive lipase (HSL) plays an important role in the regulation of rodent fat cell lipolysis. It is regarded as an adipose tissue-specific enzyme whose sole metabolic role is the catalysis of hormone-stimulated lipolysis in mammalian cells. In this report we describe the functional and structural analysis of an EstE5 protein from a soil metagenome library. Function analysis results indicated that EstE5 preferentially hydrolyzes short-chain ester compounds, and our kinetic studies revealed the optimal pH and temperature. Based on the structural analysis, we defined the active site and the binding pocket. Structurally, EstE5 belongs to the HSL family and these structural studies may have applications in the production of value-added products, including pharmaceuticals. | |||
Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase.,Nam KH, Kim MY, Kim SJ, Priyadarshi A, Lee WH, Hwang KY Biochem Biophys Res Commun. 2009 Feb 6;379(2):553-6. Epub 2008 Dec 29. PMID:19116143<ref>PMID:19116143</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3fak" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lipase 3D Structures|Lipase 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Uncultured bacterium]] | [[Category: Uncultured bacterium]] | ||
[[Category: Hwang | [[Category: Hwang KY]] | ||
[[Category: Nam | [[Category: Nam KH]] | ||
Latest revision as of 18:28, 1 November 2023
Structural and Functional Analysis of a Hormone-Sensitive Lipase like EstE5 from a Metagenome LibraryStructural and Functional Analysis of a Hormone-Sensitive Lipase like EstE5 from a Metagenome Library
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHormone-sensitive lipase (HSL) plays an important role in the regulation of rodent fat cell lipolysis. It is regarded as an adipose tissue-specific enzyme whose sole metabolic role is the catalysis of hormone-stimulated lipolysis in mammalian cells. In this report we describe the functional and structural analysis of an EstE5 protein from a soil metagenome library. Function analysis results indicated that EstE5 preferentially hydrolyzes short-chain ester compounds, and our kinetic studies revealed the optimal pH and temperature. Based on the structural analysis, we defined the active site and the binding pocket. Structurally, EstE5 belongs to the HSL family and these structural studies may have applications in the production of value-added products, including pharmaceuticals. Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase.,Nam KH, Kim MY, Kim SJ, Priyadarshi A, Lee WH, Hwang KY Biochem Biophys Res Commun. 2009 Feb 6;379(2):553-6. Epub 2008 Dec 29. PMID:19116143[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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