Structural highlights
Publication Abstract from PubMed
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.
The first crystal structure of an archaeal helical repeat protein.,Yoneda K, Sakuraba H, Tsuge H, Katunuma N, Kuramitsu S, Kawabata T, Ohshima T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):636-9. Epub 2005 Jun 30. PMID:16511116[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yoneda K, Sakuraba H, Tsuge H, Katunuma N, Kuramitsu S, Kawabata T, Ohshima T. The first crystal structure of an archaeal helical repeat protein. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):636-9. Epub 2005 Jun 30. PMID:16511116 doi:http://dx.doi.org/S1744309105019263
