Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35   Å resolution

In this study, the crystal structure of recombinant MtaL is reported at 1.35   Å resolution. Comparison of its structure with that of the truncated and cleaved MtaL present in the complex with tyrosinase directly isolated from mushroom shows that the general β -trefoil fold is conserved. However, differences are detected in the loop regions, particularly in the β 2 – β 3 loop, which is intact and not cleaved in the recombinant MtaL. Furthermore, the N-terminal tail is rotated inwards, covering the tyrosinase-binding interface. Thus, MtaL must undergo conformational changes in order to bind mature mushroom tyrosinase. Very interestingly, the β -trefoil fold has been identified to be essential for carbohydrate interaction in other lectin-like proteins. Comparison of the structures of MtaL and a ricin-B-like lectin with a bound disaccharide shows that MtaL may have a similar carbohydrate-binding site that might be involved in glycoreceptor activity.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: tyrosinase lectin tyrosinase-binding protein MtaL carbohydrate binding research communications Source Type: research

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