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Structure-based function prediction of the expanding mollusk tyrosinase family

Authors
  • Huang, Ronglian1, 2, 3
  • Li, Li1, 4
  • Zhang, Guofan1, 4
  • 1 Chinese Academy of Sciences, Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Qingdao, 266071, China , Qingdao (China)
  • 2 University of Chinese Academy of Sciences, Beijing, 100049, China , Beijing (China)
  • 3 GuangDong Ocean University, Marine Pearl Culture Lab, Fishery College, Zhanjiang, 524088, China , Zhanjiang (China)
  • 4 Qingdao National Laboratory for Marine Science and Technology, Laboratory for Marine Biology and Biotechnology, Qingdao, 266235, China , Qingdao (China)
Type
Published Article
Journal
Chinese Journal of Oceanology and Limnology
Publisher
Science Press
Publication Date
Jan 26, 2017
Volume
35
Issue
6
Pages
1454–1464
Identifiers
DOI: 10.1007/s00343-017-6066-9
Source
Springer Nature
Keywords
License
Yellow

Abstract

Tyrosinase (Ty) is a common enzyme found in many different animal groups. In our previous study, genome sequencing revealed that the Ty family is expanded in the Pacific oyster (Crassostrea gigas). Here, we examine the larger number of Ty family members in the Pacific oyster by high-level structure prediction to obtain more information about their function and evolution, especially the unknown role in biomineralization. We verified 12 Ty gene sequences from Crassostrea gigas genome and Pinctada fucata martensii transcriptome. By using phylogenetic analysis of these Tys with functionally known Tys from other molluscan species, eight subgroups were identified (CgTy_s1, CgTy_s2, MolTy_s1, MolTy-s2, MolTy-s3, PinTy-s1, PinTy-s2 and PviTy). Structural data and surface pockets of the dinuclear copper center in the eight subgroups of molluscan Ty were obtained using the latest versions of prediction online servers. Structural comparison with other Ty proteins from the protein databank revealed functionally important residues (HA1, HA2, HA3, HB1, HB2, HB3, Z1–Z9) and their location within these protein structures. The structural and chemical features of these pockets which may related to the substrate binding showed considerable variability among mollusks, which undoubtedly defines Ty substrate binding. Finally, we discuss the potential driving forces of Ty family evolution in mollusks. Based on these observations, we conclude that the Ty family has rapidly evolved as a consequence of substrate adaptation in mollusks.

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