Crystal structure of TTHA0061, an uncharacterized protein from Thermus thermophilus HB8, reveals a novel fold.
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.
Tanaka
Tomoyuki
T
RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Niwa
Hideaki
H
Yutani
Katsuhide
K
Kuramitsu
Seiki
S
Yokoyama
Shigeyuki
S
Kumarevel
Thirumananseri
T
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*
D039662:Prokaryotic Initiation Factors; D012269:Ribosomal Proteins; D018698:Glutamic Acid; D011392:Proline