Structure of a conserved CoA-binding protein synthesized by a cell-free system.
TT1466 is a hypothetical protein from the extremely thermophilic bacterium Thermus thermophilus HB8 and is highly conserved in bacteria and archaea. The selenomethionyl protein was synthesized by a cell-free system and the crystal structure was determined at 2.0 A by MAD phasing. A native crystal was used for structure refinement to 1.7 A. The structure is highly homologous to that of the CoA-binding domain of the succinyl-CoA synthetase from Escherichia coli, despite the protein having only 14% sequence identity to this domain. An isothermal titration calorimetry experiment was performed to investigate whether TT1466 binds CoA and revealed high-affinity CoA binding of TT1466.
Wada
Takashi
T
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Shirouzu
Mikako
M
Terada
Takaho
T
Ishizuka
Yoshiko
Y
Matsuda
Takayoshi
T
Kigawa
Takanori
T
Kuramitsu
Seiki
S
Park
Sam Yong
SY
Tame
Jeremy R H
JR
Yokoyama
Shigeyuki
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D002474:Cell-Free System / Q000378:metabolism; D003065:Coenzyme A / Q000737:chemistry*; D018360:Crystallography, X-Ray; D016415:Sequence Alignment; D016963:Thermus thermophilus / Q000737:chemistry
D001426:Bacterial Proteins; D003065:Coenzyme A