Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 497885
Title Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 Å resolution
Author(s) Lai, X.; Soler-Lopez, M.; Ismaya, W.T.; Wichers, H.J.; Dijkstra, B.W.
Source Acta Crystallographica Section F. Structural Biology and Crystallization Communications 72 (2016)3. - ISSN 1744-3091 - p. 244 - 250.
DOI http://dx.doi.org/10.1107/S2053230X16002107
Department(s) FBR Consumer Science & Health
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Abstract Mushroom tyrosinase-associated lectin-like protein (MtaL) binds to mature Agaricus bisporus tyrosinase in vivo, but the exact physiological function of MtaL is unknown. 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 β2-β3 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.
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