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1ffe

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(New page: 200px<br /><applet load="1ffe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ffe, resolution 1.69&Aring;" /> '''CONTRIBUTION OF CUTI...)
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[[Image:1ffe.gif|left|200px]]<br /><applet load="1ffe" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ffe, resolution 1.69&Aring;" />
 
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'''CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE'''<br />
 
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==Overview==
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==CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE==
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Cutinase from the fungus Fusarium solani pisi is a lipolytic enzyme able, to hydrolyze both aggregated and soluble substrates. It therefore provides, a powerful tool for probing the mechanisms underlying lipid hydrolysis., Lipolytic enzymes have a catalytic machinery similar to those present in, serine proteinases. It is characterized by the triad Ser, His, and Asp, (Glu) residues, by an oxyanion binding site that stabilizes the transition, state via hydrogen bonds with two main chain amide groups, and possibly by, other determinants. It has been suggested on the basis of a covalently, bond inhibitor that the cutinase oxyanion hole may consist not only of two, main chain amide groups but also of the Ser42 O gamma side chain. Among, the esterases and the serine and the cysteine proteases, only Streptomyces, scabies esterase, subtilisin, and papain, respectively, have a side chain, residue which is involved in the oxyanion hole formation. The position of, the cutinase Ser42 side chain is structurally conserved in Rhizomucor, miehei lipase with Ser82 O gamma, in Rhizopus delemar lipase with Thr83 O, gamma 1, and in Candida antartica B lipase with Thr40 O gamma 1. To, evaluate the increase in the tetrahedral intermediate stability provided, by Ser42 O gamma, we mutated Ser42 into Ala. Furthermore, since the proper, orientation of Ser42 O gamma is directed by Asn84, we mutated Asn84 into, Ala, Leu, Asp, and Trp, respectively, to investigate the contribution of, this indirect interaction to the stabilization of the oxyanion hole. The, S42A mutation resulted in a drastic decrease in the activity (450-fold), without significantly perturbing the three-dimensional structure. The N84A, and N84L mutations had milder kinetic effects and did not disrupt the, structure of the active site, whereas the N84W and N84D mutations, abolished the enzymatic activity due to drastic steric and electrostatic, effects, respectively.
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<StructureSection load='1ffe' size='340' side='right'caption='[[1ffe]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ffe]] 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=1FFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FFE FirstGlance]. <br>
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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]] 1.69&#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=1ffe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffe OCA], [https://pdbe.org/1ffe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ffe RCSB], [https://www.ebi.ac.uk/pdbsum/1ffe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffe ProSAT]</span></td></tr>
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</table>
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== Function ==
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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:8286366, PubMed:8555209, PubMed:19810726). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). 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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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/ff/1ffe_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=1ffe ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FFE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_solani_subsp._pisi Fusarium solani subsp. pisi]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FFE OCA].
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*[[Cutinase 3D structures|Cutinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state., Nicolas A, Egmond M, Verrips CT, de Vlieg J, Longhi S, Cambillau C, Martinez C, Biochemistry. 1996 Jan 16;35(2):398-410. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8555209 8555209]
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__TOC__
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[[Category: Fusarium solani subsp. pisi]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Fusarium vanettenii]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Large Structures]]
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[[Category: Cambillau, C.]]
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[[Category: Cambillau C]]
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[[Category: Martinez, C.]]
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[[Category: Martinez C]]
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[[Category: Nicolas, A.]]
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[[Category: Nicolas A]]
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[[Category: hydrolase (serine esterase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:52:38 2007''
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Current revision

CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE

PDB ID 1ffe

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