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4tgl
From Proteopedia
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| - | [[Image:4tgl.png|left|200px]] | ||
| - | + | ==CATALYSIS AT THE INTERFACE: THE ANATOMY OF A CONFORMATIONAL CHANGE IN A TRIGLYCERIDE LIPASE== | |
| + | <StructureSection load='4tgl' size='340' side='right'caption='[[4tgl]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4tgl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16457 Atcc 16457]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TGL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TGL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tgl OCA], [http://pdbe.org/4tgl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tgl RCSB], [http://www.ebi.ac.uk/pdbsum/4tgl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tgl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/tg/4tgl_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=4tgl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of an extracellular triglyceride lipase (from a fungus Rhizomucor miehei) inhibited irreversibly by diethyl p-nitrophenyl phosphate (E600) was solved by X-ray crystallographic methods and refined to a resolution of 2.65 A. The crystals are isomorphous with those of n-hexylphosphonate ethyl ester/lipase complex [Brzozowski, A. M., Derewenda, U., Derewenda, Z. S., Dodson, G. G., Lawson, D. M., Turkenburg, J. P., Bjorkling, F., Huge-Jensen, B., Patkar, S. A., & Thim, L. (1991) Nature 351, 491-494], where the conformational change was originally observed. The higher resolution of the present study allowed for a detailed analysis of the stereochemistry of the change observed in the inhibited enzyme. The movement of a 15 amino acid long "lid" (residues 82-96) is a hinge-type rigid-body motion which transports some of the atoms of a short alpha-helix (residues 85-91) by over 12 A. There are two hinge regions (residues 83-84 and 91-95) within which pronounced transitions of secondary structure between alpha and beta conformations are caused by dramatic changes of specific conformational dihedral angles (phi and psi). As a result of this change a hydrophobic area of ca. 800 A2 (8% of the total molecule surface) becomes exposed. Other triglyceride lipases are also known to have "lids" similar to the one observed in the R. miehei enzyme, and it is possible that the general stereochemistry of lipase activation at the oil-water interfaces inferred from the present X-ray study is likely to apply to the entire family of lipases. | ||
| - | + | Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase.,Derewenda U, Brzozowski AM, Lawson DM, Derewenda ZS Biochemistry. 1992 Feb 11;31(5):1532-41. PMID:1737010<ref>PMID:1737010</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4tgl" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
*[[Lipase|Lipase]] | *[[Lipase|Lipase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Atcc 16457]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
| - | [[Category: Brzozowski, A M | + | [[Category: Brzozowski, A M]] |
| - | [[Category: Derewenda, U | + | [[Category: Derewenda, U]] |
| - | [[Category: Derewenda, Z S | + | [[Category: Derewenda, Z S]] |
| - | [[Category: Lawson, D | + | [[Category: Lawson, D]] |
Current revision
CATALYSIS AT THE INTERFACE: THE ANATOMY OF A CONFORMATIONAL CHANGE IN A TRIGLYCERIDE LIPASE
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