ArticleProtein science : a publication of the Protein Society2012
Mycobacterium thermoresistibile as a source of thermostable orthologs of Mycobacterium tuberculosis proteins.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Structural and functional characterization of sulfurtransferase from Frondihabitans sp. PAMC28461.PloS one · 2024Article
- Substrate Tolerance of Bacterial Glycosyltransferase MurG: Novel Fluorescence-Based Assays.ACS infectious diseases · 2020Article
- Ab initio structure solution of a proteolytic fragment using ARCIMBOLDO.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Article
- Decoding the similarities and differences among mycobacterial species.PLoS neglected tropical diseases · 2017Article
- Engineering Archeal Surrogate Systems for the Development of Protein-Protein Interaction Inhibitors against Human RAD51.Journal of molecular biology · 2016Article
- Crystal structures of Mycobacterial MeaB and MMAA-like GTPases.Journal of structural and functional genomics · 2015Article
- Combining functional and structural genomics to sample the essential Burkholderia structome.PloS one · 2013Article
- Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of heat-stable mycobacterial proteins.Journal of bacteriology · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The genus Mycobacterium comprises major human pathogens such as the causative agent of tuberculosis, Mycobacterium tuberculosis (Mtb), and many environmental species. Tuberculosis claims ~1.5 million lives every year, and drug resistant strains of Mtb are rapidly emerging. To aid the development of new tuberculosis drugs, major efforts are currently under way to determine crystal structures of Mtb drug targets and proteins involved in pathogenicity. However, a major obstacle to obtaining crystal structures is the generation of well-diffracting crystals. Proteins from thermophiles can have better crystallization and diffraction properties than proteins from mesophiles, but their sequences and structures are often divergent. Here, we establish a thermophilic mycobacterial model organism, Mycobacterium thermoresistibile (Mth), for the study of Mtb proteins. Mth tolerates higher temperatures than Mtb or other environmental mycobacteria such as M. smegmatis. Mth proteins are on average more soluble than Mtb proteins, and comparison of the crystal structures of two pairs of orthologous proteins reveals nearly identical folds, indicating that Mth structures provide good surrogates for Mtb structures. This study introduces a thermophile as a source of protein for the study of a closely related human pathogen and marks a new approach to solving challenging mycobacterial protein structures.
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