Chemical shift assignments of CHU_1110: an AHSA1-like protein from Cytophaga hutchinsonii
- 72 Downloads
AHSA1 protein family is one of the four largest families in the Bet v1-like protein superfamily. The functions and structures of proteins in AHSA1 family are still largely unknown. CHU_1110 with 167 amino acids and a molecular weight of 19.2 kDa is a member of the AHSA1 family from Cytophaga hutchinsonii, a soil bacterium known for its ability to digest crystalline cellulose. Here we report the complete 1H, 13C and 15N chemical shift assignments of CHU_1110. The secondary structural elements of CGL2373 are consistent with the canonical AHSA1 structure. However the sequence identity of CHU_1110 with other members of AHSA1 family with functional and structural reports, such as RHE_CH02687 from Rhizobium etli, Aha1 from Homo sapiens and Yndb from Bacillus subtilis, are very low, which may suggest a different function of CHU_1110. Our chemical shift assignments of CHU_1110 are essential for the following structural and functional research of CHU_1110.
KeywordsCHU_1110 Cytophaga hutchinsonii AHSA1 Chemical shift assignments
This work was supported by funds from the National Natural Sciences Foundation of China (Grant Numbers: 21575155 and 21703283) and the Hundred Talent Program by Chinese Academy of Sciences.
Compliance with ethical standards
Conflict of interest
The authors declare that there is no conflict of interest.
- Goddard TD, Kneller DG (2008) SPARKY 3. University of California, San FransiscoGoogle Scholar
- Guntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278:353–378Google Scholar
- Koulov AV, LaPointe P, Lu B, Razvi A, Coppinger J, Dong MQ, Matteson J, Laister R, Arrowsmith C, Yates JR 3rd, Balch WE (2010) Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis. Mol Biol Cell 21:871–884CrossRefGoogle Scholar
- Neri D, Szyperski T, Otting G, Senn H, Wuethrich K (1989) Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling. Biochemistry 28:7510–7516CrossRefGoogle Scholar
- Panaretou BSG, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Hansen SN, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C (2002) Activation of the ATPase activity of Hsap90 by the stress-regulated cochaperone Aha1. Mol Cell 10:1307–1318CrossRefGoogle Scholar
- Xie G, Bruce DC, Challacombe JF, Chertkov O, Detter JC, Gilna P, Han CS, Lucas S, Misra M, Myers GL, Richardson P, Tapia R, Thayer N, Thompson LS, Brettin TS, Henrissat B, Wilson DB, McBride MJ (2007) Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii. Appl Environ Microbiol 73:3536–3546CrossRefGoogle Scholar