NMR Structure Determination and Structure-Based Functional Characterization of Conserved Hypothetical Protein MTH1175 from Methanobacterium thermoautotrophicum

  • John R. Cort
  • Adelinda Yee
  • Aled M. Edwards
  • Cheryl H. Arrowsmith
  • Michael A. Kennedy

Abstract

The solution structure of MTH1175, a 124-residue protein from the archaeon Methanobacterium thermoautotrophicum has been determined by NMR spectroscopy. MTH1175 is part of a family of conserved hypothetical proteins (COG1433) with unknown functions which contains multiple paralogs from all complete archaeal genomes and the archaeal gene-rich bacterium Thermotoga maritima. Sequence similarity indicates this protein family may be related to the nitrogen fixation proteins NifB and NifX. MTH1175 adopts an α/β topology with a single mixed β-sheet, and contains two flexible loops and an unstructured C-terminal tail. The fold resembles that of Ribonuclease H and similar proteins, but differs from these in several respects, and is not likely to have a nuclease activity.

structural genomics RNase H NMR methanobacterium thermoautotrophicum 

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Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • John R. Cort
    • 1
  • Adelinda Yee
    • 2
  • Aled M. Edwards
    • 2
    • 3
  • Cheryl H. Arrowsmith
    • 2
  • Michael A. Kennedy
    • 4
  1. 1.Environmental Molecular Sciences LaboratoryPacific Northwest National LaboratoryRichlandUSA
  2. 2.Ontario Cancer Institute and Department of Medical BiophysicsUniversity of TorontoTorontoCanada
  3. 3.Banting and Best Department of Medical Research, C. H. Best InstituteUniversity of TorontoCanada
  4. 4.Environmental Molecular Sciences LaboratoryPacific Northwest National LaboratoryRichlandUSA

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