2iw0: Difference between revisions
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Revision as of 15:12, 30 October 2007
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STRUCTURE OF THE CHITIN DEACETYLASE FROM THE FUNGAL PATHOGEN COLLETOTRICHUM LINDEMUTHIANUM
Overview
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) ... [(full description)]
About this Structure
2IW0 is a [Single protein] structure of sequence from [Glomerella lindemuthiana] with ZN, ACT, CL and PO4 as [ligands]. Active as [Chitin deacetylase], with EC number [3.5.1.41]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
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
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