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2iw0

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Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum

Structural highlights

2iw0 is a 1 chain structure with sequence from Colletotrichum lindemuthianum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.81Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iw0"

@@ Line 9: / Line 9: @@
 </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:7592838, PubMed:8987657, PubMed:9373940, PubMed:16232493, PubMed:16878976). 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:8987657, PubMed:10913295).<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>
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 15: @@
   <jmolCheckbox>
     <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>
   </jmolCheckbox>

2iw0

From Proteopedia

Current revision

Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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