Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8

Noriko Handa, Takaho Terada, Yuki Kamewari, Hiroaki Hamana, Jeremy R.H. Tame, Sam Yong Park, Kengo Kinoshita, Motonori Ota, Haruki Nakamura, Seiki Kuramitsu, Mikako Shirouzu, Shigeyuki Yokoyama

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

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 function, Rv1082 and Rv 1170 from Mycobacterium tuberculosis are enzymes involved in the mycothiol detoxification pathway. Here we report the crystal structure of the TT1542 protein at 2.0 Å resolution, which represents the first structure for this superfamily of proteins. The structure of the TT1542 monomer consists of a twisted β-sheet composed of six parallel β-strands and one antiparallel β-strand (with the strand order 3-2-1-4-5-7-6) sandwiched between six α-helices. The N-terminal five β-strands and four α-helices form an incomplete Rossmann fold-like structure. The structure shares some similarity to the sugar-processing enzymes with Rossmann fold-like domains, especially those of the GPGTF (glycogen phosphorylase/glycosyl transferase) superfamily, and also to the NAD(P)-binding Rossmann fold domains. TT1542 is a homohexamer in the crystal and in solution, the six monomers forming a cylindrical structure. Putative active sites are suggested by the structure and conserved amino acid residues.

Original languageEnglish
Pages (from-to)1621-1632
Number of pages12
JournalProtein Science
Volume12
Issue number8
DOIs
Publication statusPublished - 2003 Aug 1
Externally publishedYes

Keywords

  • Conserved protein TT1542
  • Crystallography
  • DUF158
  • GlcNAc-Ins de-N-acetylase homolog
  • GlcNAc-PI de-N-acetylase homolog
  • Mycothiol S-conjugate amidase homolog
  • Thermus thermophilus HB8

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8'. Together they form a unique fingerprint.

  • Cite this

    Handa, N., Terada, T., Kamewari, Y., Hamana, H., Tame, J. R. H., Park, S. Y., Kinoshita, K., Ota, M., Nakamura, H., Kuramitsu, S., Shirouzu, M., & Yokoyama, S. (2003). Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8. Protein Science, 12(8), 1621-1632. https://doi.org/10.1110/ps.g03104003