[Objective] The study was to analyze the structure and function of HpaGXoo and the relationship between the two.[Method] Some related bioinformatics analysis software on internet such as NPSA,Swiss-Model,SAPS and Inte...[Objective] The study was to analyze the structure and function of HpaGXoo and the relationship between the two.[Method] Some related bioinformatics analysis software on internet such as NPSA,Swiss-Model,SAPS and InterPro Scan were adopted to analyze the structure and predict its function.[Result] HpaGXoo consists of 139 amino acids,and has many alpha-helical and coiled structure,no signal peptide on N-terminal and no transmembrane structure.It locates in bacterial cytoplasm.[Conclusion] The study will lay ...展开更多
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 examin...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 Pinctadafucata martensii transcriptome. By using phylogenetic analysis of these Tys with functionally known Tys from other molluscan species, eight subgroups were identified （CgTy_sl, CgTy s2, MolTy sl, MolTy-s2, MolTy-s3, PinTy-s 1, 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, Z l-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.展开更多
基金Supported by Langfang Teachers College Research Grant(LSZB200803)~~
文摘[Objective] The study was to analyze the structure and function of HpaGXoo and the relationship between the two.[Method] Some related bioinformatics analysis software on internet such as NPSA,Swiss-Model,SAPS and InterPro Scan were adopted to analyze the structure and predict its function.[Result] HpaGXoo consists of 139 amino acids,and has many alpha-helical and coiled structure,no signal peptide on N-terminal and no transmembrane structure.It locates in bacterial cytoplasm.[Conclusion] The study will lay ...
基金Supported by the National Natural Science Foundation of China(No.31530079)the Western Pacifi c Ocean System:Structure,Dynamics and Consequences(No.XDA11000000)+1 种基金the Technological Innovation Project(No.2015ASKJ02-03,fi nancially supported by Qingdao National Laboratory for Marine Science and Technology)the Earmarked Fund for Modern Agro-Industry Technology Research System(No.CARS-48)
文摘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 Pinctadafucata martensii transcriptome. By using phylogenetic analysis of these Tys with functionally known Tys from other molluscan species, eight subgroups were identified （CgTy_sl, CgTy s2, MolTy sl, MolTy-s2, MolTy-s3, PinTy-s 1, 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, Z l-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.
