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The first structure of a protein classified in family 61 of glycoside hydrolases is presented. The crystal structure of Thielavia terrestris GH61 isoform E was determined at a resolution of 1.9 Å by Multiple Isomorphous Replacement. The fold is a β-sandwich consisting of two sheets and is a variation of the fibronectin type III fold. The structure shows significant structural similarity to the chitin-binding protein CBP21 of Serratia marscecens and shows a conserved Znbinding site which is likely to be functionally relevant. No hydrolytic activity has been reported for this protein, although it potentiates the activity of enzyme cocktails used for the degradation of cellulosic wastes. Together with the information available in the literature, serious doubts can be cast on the nature of family 61 proteins as true glycoside hydrolases, we propose instead that they have an accessory function in cellulose degradation, in analogy to the one shown for chitin binding protein.

Bacsu PerR: metal-binding sites and unambiguous highlights of 2-oxo-His in the oxidized protein