ArticleProtein science : a publication of the Protein Society2003
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Theoretical analyses on a flipping mechanism of UV-induced DNA damage.Biophysics and physicobiology · 2016Article
- Structure and function of the LmbE-like superfamily.Biomolecules · 2014Review
- Exhaustive comparison and classification of ligand-binding surfaces in proteins.Protein science : a publication of the Protein Society · 2013Article
- Catalysis by N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase (PIG-L) from Entamoeba histolytica: new roles for conserved residues.The Journal of biological chemistry · 2013Article
- N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase from Entamoeba histolytica: metal alters catalytic rates but not substrate affinity.The Journal of biological chemistry · 2011Article
- Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria.Microbiology and molecular biology reviews : MMBR · 2008Review
- eF-seek: prediction of the functional sites of proteins by searching for similar electrostatic potential and molecular surface shape.Nucleic acids research · 2007Article
- Purification, crystallization and preliminary characterization of a putative LmbE-like deacetylase from Bacillus cereus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Structures of a putative RNA 5-methyluridine methyltransferase, Thermus thermophilus TTHA1280, and its complex with S-adenosyl-L-homocysteine.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Identification of the ligand binding sites on the molecular surface of proteins.Protein science : a publication of the Protein Society · 2005Article
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12 authors.
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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.
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