1UAN

Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8

Summary for 1UAN

• Entry DOI: 10.2210/pdb1uan/pdb
• Descriptor: hypothetical protein TT1542 (2 entities in total)
• Functional Keywords: rossmann-like, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 49640.65

Authors

Handa, N.,Terada, T.,Tame, J.R.H.,Park, S.-Y.,Kinoshita, K.,Ota, M.,Nakamura, H.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-03-12, release date: 2003-08-05, Last modification date: 2023-12-27)

Primary citation

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.
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8
PROTEIN SCI., 12:1621-1632, 2003

PubMed 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 Rv1170 from Mycobacterium tuberculosis are enzymes involved in the mycothiol detoxification pathway. Here we report the crystal structure of the TT1542 protein at 2.0 A resolution, which represents the first structure for this superfamily of proteins. The structure of the TT1542 monomer consists of a twisted beta-sheet composed of six parallel beta-strands and one antiparallel beta-strand (with the strand order 3-2-1-4-5-7-6) sandwiched between six alpha-helices. The N-terminal five beta-strands and four alpha-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.

PubMed: 12876312
DOI: 10.1110/ps.g03104003

Experimental method

X-RAY DIFFRACTION (2 Å)