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1cud

From Proteopedia

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[[Image:1cud.gif|left|200px]]<br />
 
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<applet load="1cud" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cud, resolution 2.70&Aring;" />
 
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'''CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT'''<br />
 
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==Overview==
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==CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8990497 (full description)]]
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<StructureSection load='1cud' size='340' side='right'caption='[[1cud]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cud]] is a 3 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=1CUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CUD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cud OCA], [https://pdbe.org/1cud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cud RCSB], [https://www.ebi.ac.uk/pdbsum/1cud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cud ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/1cud_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1cud ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CUD 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/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]]. Structure known Active Sites: CAA, CAB and CAC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CUD OCA]].
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*[[Cutinase 3D structures|Cutinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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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]
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__TOC__
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[[Category: Fusarium solani subsp. pisi]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Fusarium vanettenii]]
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[[Category: Cambillau, C.]]
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[[Category: Large Structures]]
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[[Category: Longhi, S.]]
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[[Category: Cambillau C]]
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[[Category: glycoprotein]]
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[[Category: Longhi S]]
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[[Category: hydrolase]]
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[[Category: serine esterase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:33:12 2007''
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Current revision

CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT

PDB ID 1cud

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