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[[Image:1cuj.gif|left|200px]]<br />
<applet load="1cuj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cuj, resolution 1.60&Aring;" />
'''CUTINASE, S120C MUTANT'''<br />


==Overview==
==CUTINASE, S120C MUTANT==
In characterizing mutants and covalently inhibited complexes of Fusarium, solani cutinase, which is a 197-residue lipolytic enzyme, 34 variant, structures, crystallizing in 8 different crystal forms, have been, determined, mostly at high resolution. Taking advantage of this, considerable body of information, a structural comparative analysis was, carried out to investigate the dynamics of cutinase. Surface loops were, identified as the major flexible protein regions, particularly those, forming the active-site groove, whereas the elements constituting the, protein scaffold were found to retain the same conformation in all the, cutinase variants studied. Flexibility turned out to be correlated with, thermal motion. With a given crystal packing environment, a high, flexibility turned out to be correlated with a low involvement in crystal, packing contacts. The high degree of crystal polymorphism, which allowed, different conformations with similar energy to be detected, made it, possible to identify motions which would have remained unidentified if, only a single crystal form had been available. Fairly good agreement was, found to exist between the data obtained from the structural comparison, and those from a molecular dynamics (MD) simulation carried out on the, native enzyme. The crystallographic approach used in this study turned out, to be a suitable tool for investigating cutinase dynamics. Because of the, availability of a set of closely related proteins in different crystal, environments, the intrinsic drawback of a crystallographic approach was, bypassed. By combining several static pictures, the dynamics of the, protein could be monitored much more realistically than what can be, achieved on the basis of static pictures alone.
<StructureSection load='1cuj' size='340' side='right'caption='[[1cuj]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cuj]] 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=1CUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CUJ 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]] 1.6&#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=1cuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cuj OCA], [https://pdbe.org/1cuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cuj RCSB], [https://www.ebi.ac.uk/pdbsum/1cuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cuj 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/cu/1cuj_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=1cuj ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CUJ 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] Structure known Active Site: CAT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CUJ OCA].
*[[Cutinase 3D structures|Cutinase 3D structures]]
 
== References ==
==Reference==
<references/>
Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants., Longhi S, Nicolas A, Creveld L, Egmond M, Verrips CT, de Vlieg J, Martinez C, Cambillau C, Proteins. 1996 Dec;26(4):442-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8990497 8990497]
__TOC__
[[Category: Fusarium solani subsp. pisi]]
</StructureSection>
[[Category: Single protein]]
[[Category: Fusarium vanettenii]]
[[Category: Triacylglycerol lipase]]
[[Category: Large Structures]]
[[Category: Cambillau, C.]]
[[Category: Cambillau C]]
[[Category: Martinez, C.]]
[[Category: Martinez C]]
[[Category: glycoprotein]]
[[Category: hydrolase]]
[[Category: serine esterase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:59:56 2007''

Latest revision as of 18:43, 13 March 2024

CUTINASE, S120C MUTANTCUTINASE, S120C MUTANT

Structural highlights

1cuj 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 1.6Å
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

1cuj, resolution 1.60Å

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