1lbs

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[[Image:1lbs.jpg|left|200px]]
 
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==LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)==
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The line below this paragraph, containing "STRUCTURE_1lbs", creates the "Structure Box" on the page.
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<StructureSection load='1lbs' size='340' side='right'caption='[[1lbs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1lbs]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Moesziomyces_antarcticus Moesziomyces antarcticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LBS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEE:N-HEXYLPHOSPHONATE+ETHYL+ESTER'>HEE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1lbs| PDB=1lbs | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbs OCA], [https://pdbe.org/1lbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lbs RCSB], [https://www.ebi.ac.uk/pdbsum/1lbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lbs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIPB_PSEA2 LIPB_PSEA2] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lb/1lbs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1lbs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Many lipases are potent catalysts of stereoselective reactions and are therefore of interest for use in chemical synthesis. The crystal structures of lipases show a large variation in the shapes of their active site environments that may explain the large variation in substrate specificity of these enzymes. We have determined the three-dimensional structure of Candida antarctica lipase B (CALB) cocrystallized with the detergent Tween 80. In another crystal form, the structure of the enzyme in complex with a covalently bound phosphonate inhibitor has been determined. In both structures, the active site is exposed to the external solvent. The potential lid-forming helix alpha 5 in CALB is well-ordered in the Tween 80 structure and disordered in the inhibitor complex. The tetrahedral intermediates of two chiral substrates have been modeled on the basis of available structural and biochemical information. The results of this study provide a structural explanation for the high stereoselectivity of CALB toward many secondary alcohols.
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'''LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)'''
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Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols.,Uppenberg J, Ohrner N, Norin M, Hult K, Kleywegt GJ, Patkar S, Waagen V, Anthonsen T, Jones TA Biochemistry. 1995 Dec 26;34(51):16838-51. PMID:8527460<ref>PMID:8527460</ref>
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==Overview==
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Many lipases are potent catalysts of stereoselective reactions and are therefore of interest for use in chemical synthesis. The crystal structures of lipases show a large variation in the shapes of their active site environments that may explain the large variation in substrate specificity of these enzymes. We have determined the three-dimensional structure of Candida antarctica lipase B (CALB) cocrystallized with the detergent Tween 80. In another crystal form, the structure of the enzyme in complex with a covalently bound phosphonate inhibitor has been determined. In both structures, the active site is exposed to the external solvent. The potential lid-forming helix alpha 5 in CALB is well-ordered in the Tween 80 structure and disordered in the inhibitor complex. The tetrahedral intermediates of two chiral substrates have been modeled on the basis of available structural and biochemical information. The results of this study provide a structural explanation for the high stereoselectivity of CALB toward many secondary alcohols.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1LBS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_antarctica Candida antarctica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBS OCA].
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</div>
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<div class="pdbe-citations 1lbs" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols., Uppenberg J, Ohrner N, Norin M, Hult K, Kleywegt GJ, Patkar S, Waagen V, Anthonsen T, Jones TA, Biochemistry. 1995 Dec 26;34(51):16838-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8527460 8527460]
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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[[Category: Candida antarctica]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Triacylglycerol lipase]]
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__TOC__
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[[Category: Jones, T A.]]
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</StructureSection>
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[[Category: Uppenberg, J.]]
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[[Category: Large Structures]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:45:53 2008''
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[[Category: Moesziomyces antarcticus]]
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[[Category: Jones TA]]
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[[Category: Uppenberg J]]

Current revision

LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)

PDB ID 1lbs

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