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The first crystal structure of an archaeal helical repeat protein.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2005 Jul 01; Vol. 61 (Pt 7), pp. 636-9. Date of Electronic Publication: 2005 Jun 30. - Publication Year :
- 2005
-
Abstract
- 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 A 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 alpha-helices. A structural homology search using the DALI and MATRAS algorithms indicates that this protein can be classified as a helical repeat protein.
- Subjects :
- Algorithms
Amino Acid Sequence
Cloning, Molecular
Escherichia coli metabolism
Models, Molecular
Molecular Sequence Data
Open Reading Frames
Protein Conformation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Archaea metabolism
Archaeal Proteins chemistry
Crystallography, X-Ray methods
Sulfolobus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 61
- Issue :
- Pt 7
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 16511116
- Full Text :
- https://doi.org/10.1107/S1744309105019263