1cus

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:30, 30 October 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1cus.png|left|200px]]
 
-
<!--
+
==FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT==
-
The line below this paragraph, containing "STRUCTURE_1cus", creates the "Structure Box" on the page.
+
<StructureSection load='1cus' size='340' side='right'caption='[[1cus]], [[Resolution|resolution]] 1.25&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'>[[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>
-
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]] 1.25&#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=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>
-
{{STRUCTURE_1cus| PDB=1cus | 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/cu/1cus_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=1cus ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT===
+
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>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1cus" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_1560844}}, adds the Publication Abstract to the page
+
*[[Cutinase 3D structures|Cutinase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 1560844 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_1560844}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Fusarium vanettenii]]
-
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].
+
[[Category: Large Structures]]
-
 
+
[[Category: Cambillau C]]
-
==Reference==
+
[[Category: Martinez C]]
-
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]
+
-
[[Category: Fusarium solani subsp. pisi]]
+
-
[[Category: Single protein]]
+
-
[[Category: Cambillau, C.]]
+
-
[[Category: Martinez, C.]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:24:05 2008''
+

Current revision

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

PDB ID 1cus

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cus"
Personal tools