1tcb: Difference between revisions

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-{{Seed}}
-[[Image:1tcb.png|left|200px]]
-<!--
+==THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM CANDIDA ANTARCTICA==
-The line below this paragraph, containing "STRUCTURE_1tcb", creates the "Structure Box" on the page.
+<StructureSection load='1tcb' size='340' side='right'caption='[[1tcb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1tcb]] is a 2 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=1TCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TCB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_1tcb|  PDB=1tcb  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tcb OCA], [https://pdbe.org/1tcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tcb RCSB], [https://www.ebi.ac.uk/pdbsum/1tcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tcb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== 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/tc/1tcb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1tcb ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BACKGROUND: Lipases constitute a family of enzymes that hydrolyze triglycerides. They occur in many organisms and display a wide variety of substrate specificities. In recent years, much progress has been made towards explaining the mechanism of these enzymes and their ability to hydrolyze their substrates at an oil-water interface. RESULTS: We have determined the DNA and amino acid sequences for lipase B from the yeast Candida antarctica. The primary sequence has no significant homology to any other known lipase and deviates from the consensus sequence around the active site serine that is found in other lipases. We have determined the crystal structure of this enzyme using multiple isomorphous replacement methods for two crystal forms. Models for the orthorhombic and monoclinic crystal forms of the enzyme have been refined to 1.55 A and 2.1 A resolution, respectively. Lipase B is an alpha/beta type protein that has many features in common with previously determined lipase structures and other related enzymes. In the monoclinic crystal form, lipid-like molecules, most likely beta-octyl glucoside, can be seen close to the active site. The behaviour of these lipid molecules in the crystal structure has been studied at different pH values. CONCLUSION: The structure of Candida antarctica lipase B shows that the enzyme has a Ser-His-Asp catalytic triad in its active site. The structure appears to be in an 'open' conformation with a rather restricted entrance to the active site. We believe that this accounts for the substrate specificity and high degree of stereospecificity of this lipase.
-===THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM CANDIDA ANTARCTICA===
+The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica.,Uppenberg J, Hansen MT, Patkar S, Jones TA Structure. 1994 Apr 15;2(4):293-308. PMID:8087556<ref>PMID:8087556</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1tcb" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_8087556}}, adds the Publication Abstract to the page
+*[[Lipase 3D Structures|Lipase 3D Structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 8087556 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8087556}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-TCB is a 2 chains structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TCB OCA].
+[[Category: Moesziomyces antarcticus]]
+[[Category: Jones TA]]
-==Reference==
+[[Category: Uppenberg J]]
-<ref group="xtra">PMID:8087556</ref><references group="xtra"/>
-[[Category: Triacylglycerol lipase]]
-[[Category: Jones, T A.]]
-[[Category: Uppenberg, J.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:49:47 2009''