ArticleProtein science : a publication of the Protein Society2004
Solution structure of a novel calcium binding protein, MTH1880, from Methanobacterium thermoautotrophicum.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 11 citations in OpenAlex.
- CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation.Scientific reports · 2018Article
- Article
- The impact of extremophiles on structural genomics (and vice versa).Extremophiles : life under extreme conditions · 2008Review
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Authors and funding
5 authors at 4 institutions in 3 countries.
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Abstract
MTH1880 is a hypothetical protein from Methanobacterium thermoautotrophicum, a target organism of structural genomics. The solution structure determined by NMR spectroscopy demonstrates a typical alpha + beta-fold found in many proteins with different functions. The molecular surface of the protein reveals a small, highly acidic pocket comprising loop B (Asp36, Asp37, Asp38), the end of beta2 (Glu39), and loop D (Ser57, Ser58, Ser61), indicating that the protein would have a possible cation binding site. The NMR resonances of several amino acids within the acidic binding pocket in MTH1880, shifted upon addition of calcium ion. This calcium binding motif and overall topology of MTH1880 differ from those of other calcium binding proteins. MTH1880 did not show a calcium-induced conformational change typical of calcium sensor proteins. Therefore, we propose that the MTH1880 protein contains a novel motif for calcium-specific binding, and may function as a calcium buffering protein.
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