2iw0

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[[Image:2iw0.gif|left|200px]]<br /><applet load="2iw0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2iw0, resolution 1.81&Aring;" />
 
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'''STRUCTURE OF THE CHITIN DEACETYLASE FROM THE FUNGAL PATHOGEN COLLETOTRICHUM LINDEMUTHIANUM'''<br />
 
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==Overview==
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==Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum==
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The fungal pathogen Colletotrichum lindemuthianum secretes an endo-chitin, de-N-acetylase (ClCDA) to modify exposed hyphal chitin during penetration, and infection of plants. Although a significant amount of biochemical data, is available on fungal chitin de-N-acetylases, no structural data exist., Here we describe the 1.8 A crystal structure of a ClCDA product complex, and the analysis of the reaction mechanism using Hammett linear free, energy relationships, subsite probing, and atomic absorption spectroscopy, studies. The structural data in combination with biochemical data reveal, that ClCDA consists of a single domain encompassing a mononuclear, metalloenzyme which employs a conserved His-His-Asp zinc-binding triad, closely associated with the conserved catalytic base (aspartic acid) and, acid (histidine) to carry out acid/base catalysis. The data presented here, indicate that ClCDA possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite, affinity. Strikingly, the structure also shows that the hexahistidine, purification tag appears to form a tight interaction with the active site, groove. The enzyme requires occupancy of at least the 0 and +1 subsites by, (GlcNAc)(2) for activity and proceeds through a tetrahedral oxyanion, intermediate.
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<StructureSection load='2iw0' size='340' side='right'caption='[[2iw0]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2iw0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Colletotrichum_lindemuthianum Colletotrichum lindemuthianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IW0 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]] 1.81&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2iw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iw0 OCA], [https://pdbe.org/2iw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iw0 RCSB], [https://www.ebi.ac.uk/pdbsum/2iw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iw0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDA_COLLN CDA_COLLN] Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate (PubMed:15555935, PubMed:16232493, PubMed:16878976, PubMed:7592838, PubMed:8987657, PubMed:9373940). May play a role in evasion of the host immune response; plant chitinases liberate chitin molecules from the fungal cell wall which act as elicitors of the plant immune response, deacetylation of the liberated chitin neutralizes elicitor activity (PubMed:10913295, PubMed:8987657).<ref>PMID:15555935</ref> <ref>PMID:16232493</ref> <ref>PMID:16878976</ref> <ref>PMID:7592838</ref> <ref>PMID:8987657</ref> <ref>PMID:9373940</ref> <ref>PMID:10913295</ref> <ref>PMID:8987657</ref>
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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/iw/2iw0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2iw0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The fungal pathogen Colletotrichum lindemuthianum secretes an endo-chitin de-N-acetylase (ClCDA) to modify exposed hyphal chitin during penetration and infection of plants. Although a significant amount of biochemical data is available on fungal chitin de-N-acetylases, no structural data exist. Here we describe the 1.8 A crystal structure of a ClCDA product complex and the analysis of the reaction mechanism using Hammett linear free energy relationships, subsite probing, and atomic absorption spectroscopy studies. The structural data in combination with biochemical data reveal that ClCDA consists of a single domain encompassing a mononuclear metalloenzyme which employs a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The data presented here indicate that ClCDA possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Strikingly, the structure also shows that the hexahistidine purification tag appears to form a tight interaction with the active site groove. The enzyme requires occupancy of at least the 0 and +1 subsites by (GlcNAc)(2) for activity and proceeds through a tetrahedral oxyanion intermediate.
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==About this Structure==
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Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum.,Blair DE, Hekmat O, Schuttelkopf AW, Shrestha B, Tokuyasu K, Withers SG, van Aalten DM Biochemistry. 2006 Aug 8;45(31):9416-26. PMID:16878976<ref>PMID:16878976</ref>
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2IW0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glomerella_lindemuthiana Glomerella lindemuthiana] with ZN, ACT, CL and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chitin_deacetylase Chitin deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.41 3.5.1.41] Known structural/functional Site: <scene name='pdbsite=AC1:Po4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IW0 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum., Blair DE, Hekmat O, Schuttelkopf AW, Shrestha B, Tokuyasu K, Withers SG, van Aalten DM, Biochemistry. 2006 Aug 8;45(31):9416-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16878976 16878976]
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</div>
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[[Category: Chitin deacetylase]]
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<div class="pdbe-citations 2iw0" style="background-color:#fffaf0;"></div>
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[[Category: Glomerella lindemuthiana]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Aalten, D.M.F.Van.]]
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__TOC__
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[[Category: Blair, D.E.]]
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</StructureSection>
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[[Category: Hekmat, O.]]
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[[Category: Colletotrichum lindemuthianum]]
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[[Category: Schuttelkopf, A.W.]]
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[[Category: Large Structures]]
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[[Category: Shrestha, B.]]
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[[Category: Blair DE]]
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[[Category: Tokuyasu, K.]]
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[[Category: Hekmat O]]
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[[Category: Withers, S.G.]]
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[[Category: Schuttelkopf AW]]
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[[Category: ACT]]
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[[Category: Shrestha B]]
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[[Category: CL]]
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[[Category: Tokuyasu K]]
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[[Category: PO4]]
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[[Category: Withers SG]]
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[[Category: ZN]]
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[[Category: Van Aalten DMF]]
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[[Category: chitin de-n-acetylase]]
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[[Category: family 4 carbohydrate esterase]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:37:06 2007''
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Current revision

Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum

PDB ID 2iw0

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