Recombinant Acidianus filamentous virus 1 Putative glycosyltransferase ORF313 (ORF313)
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Q&A
FAQs for Recombinant Acidianus Filamentous Virus 1 Putative Glycosyltransferase ORF313 (ORF313)
Advanced Research Questions
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How do structural predictions for ORF313 align with functional data from related viral glycosyltransferases?
Comparative analysis with solved structures (e.g., AFV1–157 nuclease ) reveals:-
Fold conservation: Despite low sequence similarity, glycosyltransferases often share a GT-A or GT-B fold .
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Key residues: Mutational studies (e.g., alanine scanning) can validate predicted catalytic sites (Table 1).
Table 1: Predicted Functional Residues in ORF313
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What contradictions exist between genomic annotations and biochemical data for ORF313?
Methodological Guidance
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How to optimize ORF313 expression in thermophilic archaeal systems?
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What bioinformatics tools are critical for analyzing ORF313’s evolutionary relationships?
Research Gaps and Challenges
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Structural data: No crystal structure exists for ORF313, limiting mechanistic insights .
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In vivo role: Its contribution to viral fitness in extreme environments (e.g., >85°C, pH <3) remains unvalidated .
Key Citations AFV1 genome annotation and glycosyltransferase homology . AFV1 virion structure and protein-DNA interactions . Methodology for structural/functional analysis of AFV1 proteins .
