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Structure-based function prediction of the expanding mollusk tyrosinase family
Huang Ronglian1,2,4; Li Li1,3; Zhang Guofan1,3
2017-11-01
Source PublicationCHINESE JOURNAL OF OCEANOLOGY AND LIMNOLOGY
Volume35Issue:6Pages:1454-1464
SubtypeArticle
AbstractTyrosinase (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 (H-A1, H-A2, H-A3, H-B1, H-B2, H-B3, 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.
KeywordTyrosinase Mollusk Ligand Binding Pocket Substrate Diversity Evolution
DOI10.1007/s00343-017-6066-9
Indexed BySCI
Language英语
WOS IDWOS:000415810900016
Citation statistics
Document Type期刊论文
Version出版稿
Identifierhttp://ir.qdio.ac.cn/handle/337002/143285
Collection海洋生物技术研发中心
实验海洋生物学重点实验室
Affiliation1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266235, Peoples R China
4.GuangDong Ocean Univ, Marine Pearl Culture Lab, Fishery Coll, Zhanjiang 524088, Peoples R China
First Author Affilication中国科学院海洋研究所
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Huang Ronglian,Li Li,Zhang Guofan. Structure-based function prediction of the expanding mollusk tyrosinase family[J]. CHINESE JOURNAL OF OCEANOLOGY AND LIMNOLOGY,2017,35(6):1454-1464.
APA Huang Ronglian,Li Li,&Zhang Guofan.(2017).Structure-based function prediction of the expanding mollusk tyrosinase family.CHINESE JOURNAL OF OCEANOLOGY AND LIMNOLOGY,35(6),1454-1464.
MLA Huang Ronglian,et al."Structure-based function prediction of the expanding mollusk tyrosinase family".CHINESE JOURNAL OF OCEANOLOGY AND LIMNOLOGY 35.6(2017):1454-1464.
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