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Thermus thermophilus HB8  TTHA0271
60 kDa chaperonin (Protein Cpn60) (GroEL protein)

Locus: 1:complement(258408..260039)
Synonym: TT0992
DNA Sequence:
(with up/down stream)
Amino Acid Sequence:
Stop Codon: TAA
DNA Length: 1629
AA Length: 543
Mol. Weight: 57897
pI: 4.9
Absorption coefficient: 8820
Number of Methionine: 7

Expression Plasmid:
Plasmid ID:Vector:Description:Met: Distribution from DNA BANK :
PC010271-41pET-11a 7available

Expression Plasmid:Label:Purified Date:Yield (mg):

Plasmid for Gene Disruption:
BRCID:PDID:Vector:Marker Gene:Upstream:Downstream:
Reference for HTK marker: Hoseki, J. et al. (1999) J Biochem, 126, 951-6.
Reference for gene disruption: Hashimoto, Y. et al. (2001) FEBS Lett, 506, 231-4.

the most similar PDB entry:

Related Articles:
Ishii, N. and Sato, T., (2013) Anisotropic intersubunit and inter-ring interactions revealed in the native bullet-shaped chaperonin complex from Thermus thermophilus Biochim Biophys Acta   :   
Takahata, Y. et al., (2012) Close proximity of phosphorylation sites to ligand in the phosphoproteome of the extreme thermophile Thermus thermophilus HB8 Proteomics 12 :  1414-30
Kanno, R. et al., (2009) Cryo-EM Structure of the Native GroEL-GroES Complex from Thermus thermophilus Encapsulating Substrate Inside the Cavity Structure 17 :  287-293
Koike-Takeshita, A. et al., (2006) Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL J Biol Chem 281 :  962-7
Taguchi, H.(2005) Chaperonin GroEL meets the substrate protein as a "load" of the rings J Biochem 137 :  543-9
Shimamura, T. et al., (2003) Crystallization of the chaperonin GroEL-GroES complex from Thermus thermophilus HB8 Acta Crystallogr D Biol Crystallogr 59 :  1632-4
Hua, Q. et al., (2001) A thermophilic mini-chaperonin contains a conserved polypeptide-binding surface: combined crystallographic and NMR studies of the GroEL apical domain with implications for substrate interactions J Mol Biol 306 :  513-25
Taguchi, H. et al., (1997) ATP-, K+-dependent heptamer exchange reaction produces hybrids between GroEL and chaperonin from Thermus thermophilus J Biol Chem 272 :  18155-60
Amada, K. et al., (1995) Molecular cloning, expression, and characterization of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8 J Biochem 118 :  347-54
Taguchi, H. et al., (1994) Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote protein folding J Biol Chem 269 :  8529-34