The first crystal structure of an archaeal helical repeat protein
Journal Article
·
· Acta Crystallographica. Section F
- Department of Biological Science and Technology, Faculty of Engineering, University of Tokushima, Tokushima 770-8506 (Japan)
- Institute for Health Sciences, Tokushima Bunri University, Tokushima 770-8514 (Japan)
- Department of Biology, Graduate School of Science, Osaka University (Japan)
- Graduate School of Information Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0101 (Japan)
The crystal structure of ST1625p, a protein encoded by a hypothetical open reading frame ST1625 in the genome of the hyperthermophilic archaeon Sulfolobus tokodaii, was determined at 2.2 Å resolution. The structure of ST1625p consists of a unique superhelix with a low-level structure resemblance to doamins from other proteins with known three-dimensional structures. The crystal structure of ST1625p, a protein encoded by a hypothetical open reading frame ST1625 in the genome of the hyperthermophilic archaeon Sulfolobus tokodaii, was determined at 2.2 Å resolution. The only sequence similarity exhibited by the amino-acid sequence of ST1625p was a 33% identity with the sequence of SSO0983p from S. solfataricus. The 19 kDa monomeric protein was observed to consist of a right-handed superhelix assembled from a tandem repeat of ten α-helices. A structural homology search using the DALI and MATRAS algorithms indicates that this protein can be classified as a helical repeat protein.
- OSTI ID:
- 22356142
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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