1cus

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[[Image:1cus.jpg|left|200px]]
 
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{{Structure
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==FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT==
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|PDB= 1cus |SIZE=350|CAPTION= <scene name='initialview01'>1cus</scene>, resolution 1.25&Aring;
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<StructureSection load='1cus' size='340' side='right'caption='[[1cus]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1cus]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_vanettenii Fusarium vanettenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CUS FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.25&#8491;</td></tr>
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|GENE=
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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=1cus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cus OCA], [https://pdbe.org/1cus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cus RCSB], [https://www.ebi.ac.uk/pdbsum/1cus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cus ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT'''
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[https://www.uniprot.org/uniprot/CUTI1_FUSVN CUTI1_FUSVN] Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18658138, PubMed:19810726, PubMed:8286366, PubMed:8555209). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:19810726, PubMed:8286366, PubMed:8555209). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4).<ref>PMID:18658138</ref> <ref>PMID:19810726</ref> <ref>PMID:8286366</ref> <ref>PMID:8555209</ref> [PROSITE-ProRule:PRU10109]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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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/cu/1cus_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1cus ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Lipases belong to a class of esterases whose activity on triglycerides is greatly enhanced at lipid-water interfaces. This phenomenon, called interfacial activation, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic site, is displaced on substrate or inhibitor binding and probably interacts with the lipid matrix. Fusarium solani pisi cutinase belongs to a group of homologous enzymes of relative molecular mass 22-25K (ref. 7) capable of degrading cutin, the insoluble lipid-polyester matrix covering the surface of plants, and hydrolysing triglycerides. Cutinases differ from classical lipases in that they do not exhibit interfacial activation; they are active on soluble as well as on emulsified triglycerides. Cutinases therefore establish a bridge between esterases and lipases. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli. Cutinase is an alpha-beta protein; the active site is composed of the triad Ser 120, His 188 and Asp 175. Unlike other lipases, the catalytic serine is not buried under surface loops, but is accessible to solvent. This could explain why cutinase does not display interfacial activation.
Lipases belong to a class of esterases whose activity on triglycerides is greatly enhanced at lipid-water interfaces. This phenomenon, called interfacial activation, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic site, is displaced on substrate or inhibitor binding and probably interacts with the lipid matrix. Fusarium solani pisi cutinase belongs to a group of homologous enzymes of relative molecular mass 22-25K (ref. 7) capable of degrading cutin, the insoluble lipid-polyester matrix covering the surface of plants, and hydrolysing triglycerides. Cutinases differ from classical lipases in that they do not exhibit interfacial activation; they are active on soluble as well as on emulsified triglycerides. Cutinases therefore establish a bridge between esterases and lipases. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli. Cutinase is an alpha-beta protein; the active site is composed of the triad Ser 120, His 188 and Asp 175. Unlike other lipases, the catalytic serine is not buried under surface loops, but is accessible to solvent. This could explain why cutinase does not display interfacial activation.
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==About this Structure==
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Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.,Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C Nature. 1992 Apr 16;356(6370):615-8. PMID:1560844<ref>PMID:1560844</ref>
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1CUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_solani_subsp._pisi Fusarium solani subsp. pisi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent., Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C, Nature. 1992 Apr 16;356(6370):615-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1560844 1560844]
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</div>
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[[Category: Fusarium solani subsp. pisi]]
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<div class="pdbe-citations 1cus" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Cambillau, C.]]
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[[Category: Martinez, C.]]
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[[Category: hydrolase(serine esterase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:07 2008''
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==See Also==
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*[[Cutinase 3D structures|Cutinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Fusarium vanettenii]]
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[[Category: Large Structures]]
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[[Category: Cambillau C]]
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[[Category: Martinez C]]

Current revision

FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT

PDB ID 1cus

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