title: Crystal structure of TTHA0061, an uncharacterized protein from Thermus thermophilus HB8, reveals a novel fold.
abstract: The crystal structure of an uncharacterized protein TTHA0061 from Thermus thermophilus HB8, was determined and refined to 1.8 A by a single wavelength anomalous dispersion (SAD) method. The structural analysis and comparison of TTHA0061 with other existing structures in the Protein Data Bank (PDB) revealed a novel fold, suggesting that this protein may belong to a translation initiation factor or ribosomal protein family. Differential scanning calorimetry analysis suggested that the thermostability of TTHA0061 increased at pH ranges of 5.8-6.2, perhaps due to the abundance of glutamic acid residues.
authors: RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
authors: Tomoyuki
authors: T
authors: Tanaka
authors: Hideaki
authors: H
authors: Niwa
authors: Katsuhide
authors: K
authors: Yutani
authors: Seiki
authors: S
authors: Kuramitsu
authors: Shigeyuki
authors: S
authors: Yokoyama
authors: Thirumananseri
authors: T
authors: Kumarevel
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D018698:Glutamic Acid / Q000737:chemistry; D008969:Molecular Sequence Data; D039662:Prokaryotic Initiation Factors / Q000737:chemistry* / Q000235:genetics; D011392:Proline / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics; D016963:Thermus thermophilus / Q000235:genetics / Q000378:metabolism*
chemical_list: D039662:Prokaryotic Initiation Factors; D012269:Ribosomal Proteins; D018698:Glutamic Acid; D011392:Proline