ISSN:
1570-0267
Keywords:
structural genomics
;
RNase H
;
NMR
;
methanobacterium thermoautotrophicum
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1011348803324
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