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

X. Lai, M. Soler-Lopez, W.T. Ismaya, H.J. Wichers, B.W. Dijkstra

Research output: Contribution to journalArticleAcademicpeer-review

8 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)244-250
JournalActa Crystallographica Section F. Structural Biology and Crystallization Communications
Volume72
Issue number3
DOIs
Publication statusPublished - 2016

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Monophenol Monooxygenase
Agaricales
Lectins
Carrier Proteins
Crystal structure
proteins
crystal structure
Proteins
carbohydrates
Carbohydrates
Agaricus
Ricin
Disaccharides
coverings
Binding Sites

Cite this

@article{302663176d274bbabb2b2b9a8ee0c0b3,
title = "Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 {\AA} resolution",
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 {\AA} 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.",
author = "X. Lai and M. Soler-Lopez and W.T. Ismaya and H.J. Wichers and B.W. Dijkstra",
year = "2016",
doi = "10.1107/S2053230X16002107",
language = "English",
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journal = "Acta Crystallographica Section F. Structural Biology and Crystallization Communications",
issn = "1744-3091",
publisher = "International Union of Crystallography",
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}

Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 Å resolution. / Lai, X.; Soler-Lopez, M.; Ismaya, W.T.; Wichers, H.J.; Dijkstra, B.W.

In: Acta Crystallographica Section F. Structural Biology and Crystallization Communications, Vol. 72, No. 3, 2016, p. 244-250.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 Å resolution

AU - Lai, X.

AU - Soler-Lopez, M.

AU - Ismaya, W.T.

AU - Wichers, H.J.

AU - Dijkstra, B.W.

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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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DO - 10.1107/S2053230X16002107

M3 - Article

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JO - Acta Crystallographica Section F. Structural Biology and Crystallization Communications

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