1rzw
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(New page: 200px<br /><applet load="1rzw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzw" /> '''The Solution Structure of the Archaeglobus f...)
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Revision as of 23:52, 20 November 2007
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The Solution Structure of the Archaeglobus fulgidis protein AF2095. Northeast Structural Genomics Consortium target GR4
Overview
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.
About this Structure
1RZW is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
Reference
Solution structure of Archaeglobus fulgidis peptidyl-tRNA hydrolase (Pth2) provides evidence for an extensive conserved family of Pth2 enzymes in archea, bacteria, and eukaryotes., Powers R, Mirkovic N, Goldsmith-Fischman S, Acton TB, Chiang Y, Huang YJ, Ma L, Rajan PK, Cort JR, Kennedy MA, Liu J, Rost B, Honig B, Murray D, Montelione GT, Protein Sci. 2005 Nov;14(11):2849-61. PMID:16251366
Page seeded by OCA on Wed Nov 21 01:59:35 2007
Categories: Archaeoglobus fulgidus | Single protein | Acton, T.B. | Chiang, Y. | Cort, J.R. | Huang, Y.J. | Kennedy, M.A. | Liu, J. | Ma, L. | Montelione, G.T. | NESG, Northeast.Structural.Genomics.Consortium. | Powers, R. | Rost, B. | Anti-parallel beta-strands and 3 alpha-helices | Beta-sheet of 4 parallel | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi | Structural genomics
