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1cus

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Revision as of 00:26, 12 September 2015

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

Structural highlights

1cus is a 1 chain structure with sequence from Fusso. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CUTI1_FUSSO] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.,Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C Nature. 1992 Apr 16;356(6370):615-8. PMID:1560844^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature. 1992 Apr 16;356(6370):615-8. PMID:1560844 doi:http://dx.doi.org/10.1038/356615a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Fusso | Cambillau, C | Martinez, C

@@ Line 2: / Line 2: @@
 <StructureSection load='1cus' size='340' side='right' caption='[[1cus]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cus]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nectria_haematococca_mpvi Nectria haematococca mpvi]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CUS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cus]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fusso Fusso]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CUS FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cus OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cus RCSB], [http://www.ebi.ac.uk/pdbsum/1cus PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cus OCA], [http://pdbe.org/1cus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cus RCSB], [http://www.ebi.ac.uk/pdbsum/1cus PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 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==
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Nectria haematococca mpvi]]
+[[Category: Fusso]]
 [[Category: Cambillau, C]]
 [[Category: Martinez, C]]

1cus

From Proteopedia

Revision as of 00:26, 12 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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