|Protein Science (2005) 14(11):2849-61|
|Northeast Structural Genomics Consortium|
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The solution structure of protein AF2095 from the thermophilic archaea Archaeglobus fulgidis, a 123-residue (13.6-kDa) protein, has been determined by NMR methods. ...
The structure of AF2095 is comprised of four alpha-helices and a mixed beta-sheet consisting of four parallel and anti-parallel beta-strands, where the alpha-helices sandwich the beta-sheet. Sequence and structural comparison of AF2095 with proteins from Homo sapiens, Methanocaldococcus jannaschii, and Sulfolobus solfataricus reveals that AF2095 is a peptidyl-tRNA hydrolase (Pth2). This structural comparison also identifies putative catalytic residues and a tRNA interaction region for AF2095. The structure of AF2095 is also similar to the structure of protein TA0108 from archaea Thermoplasma acidophilum, which is deposited in the Protein Data Bank but not functionally annotated. The NMR structure of AF2095 has been further leveraged to obtain good-quality structural models for 55 other proteins. Although earlier studies have proposed that the Pth2 protein family is restricted to archeal and eukaryotic organisms, the similarity of the AF2095 structure to human Pth2, the conservation of key active-site residues, and the good quality of the resulting homology models demonstrate a large family of homologous Pth2 proteins that are conserved in eukaryotic, archaeal, and bacterial organisms, providing novel insights in the evolution of the Pth and Pth2 enzyme families.
|classification enzymology chemistry |
|Carboxylic Ester Hydrolases Models, Molecular Archaeal Proteins Phylogeny Conserved Sequence Humans Evolution, Molecular Binding Sites Nuclear Magnetic Resonance, Biomolecular Sequence Homology, Amino Acid Archaeoglobus fulgidus Bacteria Structural Homology, Protein Solutions Archaea |
|20 (Last update: 04/01/2017 11:38:43am)|
|Protein Sci. 2005 Nov;14(11):2849-61.|