The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus

• Published in: The EMBO journal Vol. 20; no. 3; pp. 562 - 569
• Main Authors: Kawaguchi, Shin-ichi, Müller, Jörg, Linde, Dirk, Kuramitsu, Seiki, Shibata, Takehiko, Inoue, Yorinao, Vassylyev, Dmitry G., Yokoyama, Shigeyuki
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.02.2001; Blackwell Publishing Ltd; Oxford University Press
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Base Sequence; chaperone; chaperones; crystal structure; Crystallography, X-Ray; CsaA protein; Dimerization; DNA Primers - genetics; Models, Molecular; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Sequence Data; protein export; Protein Structure, Quaternary; Protein Subunits; Sequence Homology, Amino Acid; Thermus thermophilus; Thermus thermophilus - chemistry; Thermus thermophilus - genetics; tRNA; ttCsaA protein

The CsaA protein was first characterized in Bacillus subtilis as a molecular chaperone with export‐related activities. Here we report the 2.0 Å‐resolution crystal structure of the Thermus thermophilus CsaA protein, designated ttCsaA. Atomic structure and experiments in solution revealed a homodimer...