1ffd: Difference between revisions

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-{{Seed}}
-[[Image:1ffd.png|left|200px]]
-<!--
+==CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE==
-The line below this paragraph, containing "STRUCTURE_1ffd", creates the "Structure Box" on the page.
+<StructureSection load='1ffd' size='340' side='right'caption='[[1ffd]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ffd]] 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=1FFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FFD FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ffd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffd OCA], [https://pdbe.org/1ffd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ffd RCSB], [https://www.ebi.ac.uk/pdbsum/1ffd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffd ProSAT]</span></td></tr>
-{{STRUCTURE_1ffd|  PDB=1ffd  |  SCENE=  }}
+</table>
+== Function ==
+[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]
+== 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/ff/1ffd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ffd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE===
+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:8555209<ref>PMID:8555209</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1ffd" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_8555209}}, adds the Publication Abstract to the page
+*[[Cutinase 3D structures|Cutinase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 8555209 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8555209}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Fusarium vanettenii]]
-FFD is a 1 chain 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=1FFD OCA].
+[[Category: Large Structures]]
+[[Category: Cambillau C]]
-==Reference==
+[[Category: Martinez C]]
-<ref group="xtra">PMID:8555209</ref><references group="xtra"/>
+[[Category: Nicolas A]]
-[[Category: Fusarium solani subsp. pisi]]
-[[Category: Triacylglycerol lipase]]
-[[Category: Cambillau, C.]]
-[[Category: Martinez, C.]]
-[[Category: Nicolas, A.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:01:50 2009''