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1trh

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[[Image:1trh.gif|left|200px]]
 
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==TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE==
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The line below this paragraph, containing "STRUCTURE_1trh", creates the "Structure Box" on the page.
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<StructureSection load='1trh' size='340' side='right'caption='[[1trh]], [[Resolution|resolution]] 2.10&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'>[[1trh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Diutina_rugosa Diutina rugosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TRH 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]] 2.1&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1trh| PDB=1trh | 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=1trh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1trh OCA], [https://pdbe.org/1trh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1trh RCSB], [https://www.ebi.ac.uk/pdbsum/1trh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1trh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIP1_DIURU LIP1_DIURU]
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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/tr/1trh_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=1trh ConSurf].
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<div style="clear:both"></div>
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'''TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE'''
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The structure of Candida rugosa lipase in a new crystal form has been determined and refined at 2.1 A resolution. The lipase molecule was found in an inactive conformation, with the active site shielded from the solvent by a part of the polypeptide chain-the flap. Comparison of this structure with the previously determined "open" form of this lipase, in which the active site is accessible to the solvent and presumably the substrate, shows that the transition between these 2 states requires only movement of the flap. The backbone NH groups forming the putative oxyanion hole do not change position during this rearrangement, indicating that this feature is preformed in the inactive state. The 2 lipase conformations probably correspond to states at opposite ends of the pathway of interfacial activation. Quantitative analysis indicates a large increase of the hydrophobic surface in the vicinity of the active site. The flap undergoes a flexible rearrangement during which some of its secondary structure refolds. The interactions of the flap with the rest of the protein change from mostly hydrophobic in the inactive form to largely hydrophilic in the "open" conformation. Although the flap movement cannot be described as a rigid body motion, it has very definite hinge points at Glu 66 and at Pro 92. The rearrangement is accompanied by a cis-trans isomerization of this proline, which likely increases the energy required for the transition between the 2 states, and may play a role in the stabilization of the active conformation at the water/lipid interface. Carbohydrate attached at Asn 351 also provides stabilization for the open conformation of the flap.
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[[Category: Diutina rugosa]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Cygler M]]
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1TRH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_rugosa Candida rugosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRH OCA].
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[[Category: Grochulski P]]
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==Reference==
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Two conformational states of Candida rugosa lipase., Grochulski P, Li Y, Schrag JD, Cygler M, Protein Sci. 1994 Jan;3(1):82-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8142901 8142901]
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[[Category: Candida rugosa]]
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[[Category: Single protein]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Cygler, M.]]
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[[Category: Grochulski, P.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:17:18 2008''
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Current revision

TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE

PDB ID 1trh

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