Crystal structure of a novel fold protein Gp72 from the freshwater cyanophage Mic1
Autor: | Wei-Fang Li, Yan-Yan Zhao, Hua Jin, Yong-Liang Jiang, Zhi-Peng Chen, Qiong Li, Yuxing Chen, Ying Wang, Feng Yang, Cong-Zhao Zhou |
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Rok vydání: | 2019 |
Předmět: |
Cyanobacteria
Models Molecular Protein Conformation alpha-Helical Protein Folding Hypothetical protein Genetic Vectors Gene Expression Fresh Water Crystal structure Crystallography X-Ray Biochemistry 03 medical and health sciences Viral Proteins Structural Biology Escherichia coli Bacteriophages Protein Interaction Domains and Motifs Amino Acid Sequence Disulfides Cloning Molecular Cyanophages Molecular Biology 030304 developmental biology Genetics 0303 health sciences Binding Sites biology Sequence Homology Amino Acid Chemistry 030302 biochemistry & molecular biology Disulfide bond Cyanophage Protein superfamily biology.organism_classification Recombinant Proteins Protein Conformation beta-Strand Protein Multimerization Oxidation-Reduction Sequence Alignment Protein Binding |
Zdroj: | ProteinsREFERENCES. 88(9) |
ISSN: | 1097-0134 |
Popis: | Cyanophages, widespread in aquatic systems, are a class of viruses that specifically infect cyanobacteria. Though they play important roles in modulating the homeostasis of cyanobacterial populations, little is known about the freshwater cyanophages, especially those hypothetical proteins of unknown function. Mic1 is a freshwater siphocyanophage isolated from the Lake Chaohu. It encodes three hypothetical proteins Gp65, Gp66, and Gp72, which share an identity of 61.6% to 83%. However, we find these three homologous proteins differ from each other in oligomeric state. Moreover, we solve the crystal structure of Gp72 at 2.3 A, which represents a novel fold in the α + β class. Structural analyses combined with redox assays enable us to propose a model of disulfide bond mediated oligomerization for Gp72. Altogether, these findings provide structural and biochemical basis for further investigations on the freshwater cyanophage Mic1. |
Databáze: | OpenAIRE |
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