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| - | ==STRUCTURE OF THE CHITIN DEACETYLASE FROM THE FUNGAL PATHOGEN COLLETOTRICHUM LINDEMUTHIANUM== | + | |
| - | <StructureSection load='2iw0' size='340' side='right' caption='[[2iw0]], [[Resolution|resolution]] 1.81Å' scene=''> | + | ==Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum== |
| | + | <StructureSection load='2iw0' size='340' side='right'caption='[[2iw0]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bean_anthracnose_fungus Bean anthracnose fungus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IW0 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <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> |
| - | <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=2iw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iw0 OCA], [http://pdbe.org/2iw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iw0 RCSB], [http://www.ebi.ac.uk/pdbsum/2iw0 PDBsum]</span></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=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> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/2iw0_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/2iw0_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | + | </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]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bean anthracnose fungus]] | + | [[Category: Colletotrichum lindemuthianum]] |
| - | [[Category: Chitin deacetylase]] | + | [[Category: Large Structures]] |
| - | [[Category: Aalten, D M.F Van]]
| + | [[Category: Blair DE]] |
| - | [[Category: Blair, D E]] | + | [[Category: Hekmat O]] |
| - | [[Category: Hekmat, O]] | + | [[Category: Schuttelkopf AW]] |
| - | [[Category: Schuttelkopf, A W]] | + | [[Category: Shrestha B]] |
| - | [[Category: Shrestha, B]] | + | [[Category: Tokuyasu K]] |
| - | [[Category: Tokuyasu, K]] | + | [[Category: Withers SG]] |
| - | [[Category: Withers, S G]] | + | [[Category: Van Aalten DMF]] |
| - | [[Category: Chitin de-n-acetylase]] | + | |
| - | [[Category: Family 4 carbohydrate esterase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4] [5] [6] [7] [8]
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
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.
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[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shrestha B, Blondeau K, Stevens WF, Hegarat FL. Expression of chitin deacetylase from Colletotrichum lindemuthianum in Pichia pastoris: purification and characterization. Protein Expr Purif. 2004 Dec;38(2):196-204. PMID:15555935 doi:10.1016/j.pep.2004.08.012
- ↑ Tokuyasu K, Ohnishi-Kameyama M, Hayashi K, Mori Y. Cloning and expression of chitin deacetylase gene from a Deuteromycete, Colletotrichum lindemuthianum. J Biosci Bioeng. 1999;87(4):418-23. PMID:16232493 doi:10.1016/s1389-1723(99)80088-7
- ↑ Blair DE, Hekmat O, Schuttelkopf AW, Shrestha B, Tokuyasu K, Withers SG, van Aalten DM. Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum. Biochemistry. 2006 Aug 8;45(31):9416-26. PMID:16878976 doi:10.1021/bi0606694
- ↑ Tsigos I, Bouriotis V. Purification and characterization of chitin deacetylase from Colletotrichum lindemuthianum. J Biol Chem. 1995 Nov 3;270(44):26286-91. PMID:7592838 doi:10.1074/jbc.270.44.26286
- ↑ Tokuyasu K, Ohnishi-Kameyama M, Hayashi K. Purification and characterization of extracellular chin deacetylase from Colletotrichum lindemuthianum. Biosci Biotechnol Biochem. 1996 Oct;60(10):1598-603. PMID:8987657 doi:10.1271/bbb.60.1598
- ↑ Tokuyasu K, Ono H, Ohnishi-Kameyama M, Hayashi K, Mori Y. Deacetylation of chitin oligosaccharides of dp 2-4 by chitin deacetylase from Colletotrichum lindemuthianum. Carbohydr Res. 1997 Sep 26;303(3):353-8. PMID:9373940 doi:10.1016/s0008-6215(97)00166-3
- ↑ Tokuyasu K, Mitsutomi M, Yamaguchi I, Hayashi K, Mori Y. Recognition of chitooligosaccharides and their N-acetyl groups by putative subsites of chitin deacetylase from a deuteromycete, Colletotrichum lindemuthianum. Biochemistry. 2000 Aug 1;39(30):8837-43. PMID:10913295 doi:10.1021/bi0005355
- ↑ Tokuyasu K, Ohnishi-Kameyama M, Hayashi K. Purification and characterization of extracellular chin deacetylase from Colletotrichum lindemuthianum. Biosci Biotechnol Biochem. 1996 Oct;60(10):1598-603. PMID:8987657 doi:10.1271/bbb.60.1598
- ↑ Blair DE, Hekmat O, Schuttelkopf AW, Shrestha B, Tokuyasu K, Withers SG, van Aalten DM. Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum. Biochemistry. 2006 Aug 8;45(31):9416-26. PMID:16878976 doi:10.1021/bi0606694
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