Purification and Backbone Assignment of the Hypothetical Protein MTH1821 from Methanobacterium Thermoautotrophicum H

  • Kwak, Soo-Young (Department of Biochemistry, HTSD-NMR National Research Laboratory, College of Science, Yonsei University) ;
  • Lee, Woong-Hee (Department of Biochemistry, HTSD-NMR National Research Laboratory, College of Science, Yonsei University) ;
  • Shin, Joon (Department of Biochemistry, HTSD-NMR National Research Laboratory, College of Science, Yonsei University) ;
  • Ko, Sung-Geon (Department of Biochemistry, HTSD-NMR National Research Laboratory, College of Science, Yonsei University) ;
  • Lee, Weon-Tae (Department of Biochemistry, HTSD-NMR National Research Laboratory, College of Science, Yonsei University)
  • Published : 2007.12.20

Abstract

MTH1821 (UniProtKB/TrEMBL ID O27849) is a 96-residue hypothetical protein from the open reading frame of Methanobacterium thermoautotrophicum H one of the target organisms of structural genomics pilot project. Proteins which contain conserved sequence compared with MTH1821 have not been discovered yet and the functional and structural information for MTH1821 is not available. Here, we present the sequence-specific backbone resonance using multidimensional heteronuc1ear NMR spectroscopy and propose the secondary structure using GetSBY software. The backbone resonances of N, HN, $C_{\alpha}$, $C_{\beta}$, CO and $H_{\alpha}$ which are necessary for a prediction of secondary structure by GetSBY were assigned about 98% (557/568). The secondary structure of MTH1821 confirmed that it is comprised of four strand regions and two helical regions. This report will provide a valuable resource for the calculation solution structure of MTH1821 and for the other hypothetical protein that is targeted for structural-based functional discovery.

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