Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8.

  title={Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8.},
  author={Noriko Handa and Takaho Terada and Yuki Kamewari and Hiroaki Hamana and Jeremy R. H. Tame and Sam-Yong Park and Kengo Kinoshita and Motonori Ota and Haruki Nakamura and Seiki Kuramitsu and Mikako Shirouzu and Shigeyuki Yokoyama},
  journal={Protein science : a publication of the Protein Society},
  volume={12 8},
The TT1542 protein from Thermus thermophilus HB8 is annotated as a conserved hypothetical protein, and belongs to the DUF158 family in the Pfam database. A BLAST search revealed that homologs of TT1542 are present in a wide range of organisms. The TT1542 homologs in eukaryotes, PIG-L in mammals, and GPI12 in yeast and protozoa, have N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) de-N-acetylase activity. Although most of the homologs in prokaryotes are hypothetical and have no known… CONTINUE READING


Publications citing this paper.
Showing 1-8 of 8 extracted citations


Publications referenced by this paper.
Showing 1-10 of 46 references

Dali/FSSP classification of three-dimensional protein folds

Nucleic Acids Research • 1997
View 5 Excerpts
Highly Influenced

ARP/wARP and molecular replacement.

Acta crystallographica. Section D, Biological crystallography • 2001
View 2 Excerpts
Highly Influenced

PROCHECK: A program to check the stereochemical quality of protein structures

R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton
J. Appl. Crystallogr. 26: 283–291. • 1992
View 2 Excerpts
Highly Influenced

Numerical calculations of electrostatic potentials of protein–solvent systems by the self consistent boundary method

H. Nakamura, S. Nishida
J. Phys. Soc. Jpn. 56: 1609–1622. • 1989
View 1 Excerpt
Highly Influenced

The classification of amino acid conservation

W. Taylor
J. Theor. Biol. 119: 205–218. • 1986
View 3 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…