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Crystal structure of a novel fold protein Gp72 from the freshwater cyanophage Mic1
- Source :
- ProteinsREFERENCES. 88(9)
- Publication Year :
- 2019
-
Abstract
- 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.
- Subjects :
- 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
Subjects
Details
- ISSN :
- 10970134
- Volume :
- 88
- Issue :
- 9
- Database :
- OpenAIRE
- Journal :
- ProteinsREFERENCES
- Accession number :
- edsair.doi.dedup.....991e186f45eb9f90223ec817a0cafc2a