1tic

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[[Image:1tic.gif|left|200px]]
 
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==CONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMAR==
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The line below this paragraph, containing "STRUCTURE_1tic", creates the "Structure Box" on the page.
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<StructureSection load='1tic' size='340' side='right'caption='[[1tic]], [[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'>[[1tic]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizopus_arrhizus Rhizopus arrhizus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TIC 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tic OCA], [https://pdbe.org/1tic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tic RCSB], [https://www.ebi.ac.uk/pdbsum/1tic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tic ProSAT]</span></td></tr>
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{{STRUCTURE_1tic| PDB=1tic | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIP_RHIOR LIP_RHIOR] Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity.<ref>PMID:11506890</ref>
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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/ti/1tic_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1tic ConSurf].
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<div style="clear:both"></div>
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'''CONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMAR'''
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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==Overview==
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<references/>
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Considerable controversy exists regarding the exact nature of the molecular mechanism of interfacial activation, a process by which most lipases achieve maximum catalytic activity upon adsorption to an oil water interface. X-ray crystallographic studies show that lipases contain buried active centers and that displacements of entire secondary structure elements, or "lids," take place when the enzymes assume active conformations [Derewenda, U., A. M. Brzozowski, D. M. Lawson, and Z. S. Derewenda. 1992. Biochemistry: 31: 1532-1541; van Tilbeurgh, H., M-P. Egloff, C. Martinez, N. Rugani, R. Verger, and C. Cambillau. 1993. Nature: 362: 814-820; Grochulski, P., L. Yunge, J. D. Schrag, F. Bouthillier, P. Smith, D. Harrison, B. Rubin, and M. Cygler. 1993. J. Biol. Chem. 268: 12843-12847]. A simple two-state model inferred from these results implies that the "closed" conformation is stable in an aqueous medium, rendering the active centers inaccessible to water soluble substrates. We now report that in crystals of the Humicola lanuginosa lipase the "lid" is significantly disordered irrespective of the ionic strength of the medium, while in a related enzyme from Rhizopus delemar, crystallized in the presence of a detergent, the two molecules that form the asymmetric unit show different "lid" conformations. These new results call into question the simplicity of the "enzyme theory" of interfacial activation.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1TIC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhizopus_oryzae Rhizopus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIC OCA].
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[[Category: Rhizopus arrhizus]]
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[[Category: Derewenda U]]
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==Reference==
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[[Category: Derewenda ZS]]
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Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar., Derewenda U, Swenson L, Wei Y, Green R, Kobos PM, Joerger R, Haas MJ, Derewenda ZS, J Lipid Res. 1994 Mar;35(3):524-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8014587 8014587]
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[[Category: Green R]]
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[[Category: Rhizopus oryzae]]
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[[Category: Haas MJ]]
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[[Category: Single protein]]
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[[Category: Joerger R]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Swenson L]]
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[[Category: Derewenda, U.]]
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[[Category: Derewenda, Z S.]]
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[[Category: Green, R.]]
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[[Category: Haas, M J.]]
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[[Category: Joerger, R.]]
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[[Category: Swenson, L.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:58:50 2008''
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Current revision

CONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMAR

PDB ID 1tic

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