Skip to main content
Log in

Chemical shift assignments of CHU_1110: an AHSA1-like protein from Cytophaga hutchinsonii

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293

    Article  Google Scholar 

  • Goddard TD, Kneller DG (2008) SPARKY 3. University of California, San Fransisco

    Google Scholar 

  • Guntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278:353–378

    Google 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 21:871–884

    Article  Google Scholar 

  • Liang C, Zhu J, Hu R, Ramelot TA, Kennedy MA, Liu M, Yang Y (2017) Solution NMR structure of RHE_CH02687 from Rhizobium etli: a novel flavonoid-binding protein. Proteins 85:951–956

    Article  Google Scholar 

  • Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 23:1402–1410

    Article  Google 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 28:7510–7516

    Article  Google 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 10:1307–1318

    Article  Google Scholar 

  • Shen Y, Bax A (2013) Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J Biomol NMR 56:227–241

    Article  Google Scholar 

  • Stark JL, Mercier KA, Mueller GA, Acton TB, Xiao R, Montelione GT, Powers R (2010) Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilis. Proteins 78:3328–3340

    Article  Google 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 73:3536–3546

    Article  Google Scholar 

  • Zhu Y, McBride MJ (2017) The unusual cellulose utilization system of the aerobic soil bacterium Cytophaga hutchinsonii. Appl Microbiol Biotechnol 101:7113–7127

    Article  Google Scholar 

Download references

Acknowledgements

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.

Author information

Authors and Affiliations

Authors

Corresponding authors

Correspondence to Jiang Zhu or Maili Liu.

Ethics declarations

Conflict of interest

The authors declare that there is no conflict of interest.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Liang, C., He, T., Li, T. et al. Chemical shift assignments of CHU_1110: an AHSA1-like protein from Cytophaga hutchinsonii. Biomol NMR Assign 12, 155–158 (2018). https://doi.org/10.1007/s12104-018-9799-2

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-018-9799-2

Keywords

Navigation