1agy: Difference between revisions

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[[Image:1agy.png|left|200px]]


{{STRUCTURE_1agy| PDB=1agy | SCENE= }}
==The 1.15 angstrom refined structure of fusarium solani pisi cutinase==
<StructureSection load='1agy' size='340' side='right'caption='[[1agy]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1agy]] 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=1AGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AGY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#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=1agy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1agy OCA], [https://pdbe.org/1agy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1agy RCSB], [https://www.ebi.ac.uk/pdbsum/1agy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1agy ProSAT]</span></td></tr>
</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: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]
== 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/ag/1agy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1agy ConSurf].
<div style="clear:both"></div>


===The 1.15 angstrom refined structure of fusarium solani pisi cutinase===
==See Also==
 
*[[Cutinase 3D structures|Cutinase 3D structures]]
{{ABSTRACT_PUBMED_9175860}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1agy]] 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=1AGY OCA].
</StructureSection>
 
[[Category: Fusarium vanettenii]]
==Reference==
[[Category: Large Structures]]
<ref group="xtra">PMID:009175860</ref><references group="xtra"/>
[[Category: Cambillau C]]
[[Category: Nectria haematococca mpvi]]
[[Category: Martinez C]]
[[Category: Cambillau, C.]]
[[Category: Nicolas A]]
[[Category: Martinez, C.]]
[[Category: Nicolas, A.]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Serine esterase]]

Latest revision as of 18:24, 13 March 2024

The 1.15 angstrom refined structure of fusarium solani pisi cutinaseThe 1.15 angstrom refined structure of fusarium solani pisi cutinase

Structural highlights

1agy is a 1 chain structure with sequence from Fusarium vanettenii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.15Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3] [4] [PROSITE-ProRule:PRU10109]

Evolutionary Conservation

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

See Also

References

  1. ↑ Chen S, Tong X, Woodard RW, Du G, Wu J, Chen J. Identification and characterization of bacterial cutinase. J Biol Chem. 2008 Sep 19;283(38):25854-62. PMID:18658138 doi:10.1074/jbc.M800848200
  2. ↑ Liu Z, Gosser Y, Baker PJ, Ravee Y, Lu Z, Alemu G, Li H, Butterfoss GL, Kong XP, Gross R, Montclare JK. Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation. J Am Chem Soc. 2009 Nov 4;131(43):15711-6. PMID:19810726 doi:10.1021/ja9046697
  3. ↑ Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C. Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry. 1994 Jan 11;33(1):83-9. PMID:8286366
  4. ↑ Nicolas A, Egmond M, Verrips CT, de Vlieg J, Longhi S, Cambillau C, Martinez C. Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Biochemistry. 1996 Jan 16;35(2):398-410. PMID:8555209 doi:http://dx.doi.org/10.1021/bi9515578

1agy, resolution 1.15Å

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