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The first crystal structure of an archaeal helical repeat protein.

Authors :
Yoneda K
Sakuraba H
Tsuge H
Katunuma N
Kuramitsu S
Kawabata T
Ohshima T
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.

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