Crystal structure of AFV1-102, a protein from the acidianus filamentous virus 1
β Scribed by Jenny Keller; Nicolas Leulliot; Bruno Collinet; Valerie Campanacci; Christian Cambillau; David Pranghisvilli; Herman van Tilbeurgh
- Book ID
- 105356769
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2009
- Tongue
- English
- Weight
- 348 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0961-8368
- DOI
- 10.1002/pro.79
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β¦ Synopsis
Abstract
Viruses infecting hyperthermophilic archaea have intriguing morphologies and genomic properties. The vast majority of their genes do not have homologs other than in other hyperthermophilic viruses, and the biology of these viruses is poorly understood. As part of a structural genomics project on the proteins of these viruses, we present here the structure of a 102 amino acid protein from acidianus filamentous virus 1 (AFV1β102). The structure shows that it is made of two identical motifs that have poor sequence similarity. Although no function can be proposed from structural analysis, tight binding of the gateway tag peptide in a groove between the two motifs suggests AFV1β102 is involved in protein protein interactions.
π SIMILAR VOLUMES
## Abstract Bacteriophage QΞ² is a small RNA virus that infects __Escherichia coli.__ The virus particle contains a few copies of the minor coat protein A1, a Cβterminally prolonged version of the coat protein, which is formed when ribosomes occasionally readβthrough the leaky stop codon of the coat