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1cvl

From Proteopedia

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[[Image:1cvl.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF BACTERIAL LIPASE FROM CHROMOBACTERIUM VISCOSUM ATCC 6918==
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|PDB= 1cvl |SIZE=350|CAPTION= <scene name='initialview01'>1cvl</scene>, resolution 1.6&Aring;
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<StructureSection load='1cvl' size='340' side='right'caption='[[1cvl]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ACT:The+Catalytic+Triad+Of+Active+Center+Consists+Of+Residue+...'>ACT</scene>, <scene name='pdbsite=CA:Ca+Binding+Site'>CA</scene> and <scene name='pdbsite=OXY:Performed+Oxyanion,+Stabilized+By+The+Amide+N+Atoms+Of+L+...'>OXY</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[1cvl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_viscosum Chromobacterium viscosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CVL FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 1.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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}}
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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=1cvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvl OCA], [https://pdbe.org/1cvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cvl RCSB], [https://www.ebi.ac.uk/pdbsum/1cvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cvl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIP_PSEPS LIP_PSEPS] Catalyzes the hydrolysis of triacylglycerol.<ref>PMID:7786905</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/cv/1cvl_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=1cvl ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF BACTERIAL LIPASE FROM CHROMOBACTERIUM VISCOSUM ATCC 6918'''
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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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The crystal structure of a lipase from the bacterium Chromobacterium viscosum ATCC 6918 (CVL) has been determined by isomorphous replacement and refined at 1.6 angstroms resolution to an R-factor of 17.8%. The lipase has the overall topology of an alpha/beta type protein, which was also found for previously determined lipase structures. The catalytic triad of the active center consists of the residues Ser87, Asp263 and His285. These residues are not exposed to the solvent, but a narrow channel connects them with the molecular surface. This conformation is very similar to the previously reported closed conformation of Pseudomonas glumae lipase (PGL), but superposition of the two lipase structures reveals several conformational differences. r.m.s. deviations greater than 2 angstroms are found for the C alpha-atoms of the polypeptide chains from His15 to Asp28, from Leu49 to Ser54 and from Lys128 to Gln158. Compared to the PGL structure in the CVL structure, three alpha-helical fragments are shorter, one beta-strand is longer and an additional antiparallel beta-sheet is found. In contrast to PGL, CVL displays an oxyanion hole, which is stabilized by the amide nitrogen atoms of Leu17 and Gln88, and a cis-peptide bond between Gln291 and Leu292. CVL contains a Ca2+, like the PGL, which is coordinated by four oxygen atoms from the protein and two water molecules.
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__TOC__
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</StructureSection>
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==About this Structure==
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1CVL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chromobacterium_viscosum Chromobacterium viscosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVL OCA].
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==Reference==
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Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution., Lang D, Hofmann B, Haalck L, Hecht HJ, Spener F, Schmid RD, Schomburg D, J Mol Biol. 1996 Jun 21;259(4):704-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8683577 8683577]
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[[Category: Chromobacterium viscosum]]
[[Category: Chromobacterium viscosum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Haalck L]]
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[[Category: Haalck, L.]]
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[[Category: Hecht H-J]]
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[[Category: Hecht, H J.]]
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[[Category: Hofmann B]]
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[[Category: Hofmann, B.]]
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[[Category: Lang DA]]
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[[Category: Lang, D A.]]
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[[Category: Schmid RD]]
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[[Category: Schmid, R D.]]
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[[Category: Schomburg D]]
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[[Category: Schomburg, D.]]
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[[Category: Spener F]]
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[[Category: Spener, F.]]
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[[Category: CA]]
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[[Category: cis-peptide]]
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[[Category: hydrolase]]
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[[Category: oxyanion]]
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[[Category: pseudomonadaceae]]
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[[Category: triacylglycerol-hydrolase]]
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[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:27 2008''
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Current revision

CRYSTAL STRUCTURE OF BACTERIAL LIPASE FROM CHROMOBACTERIUM VISCOSUM ATCC 6918

PDB ID 1cvl

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