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1rzw
From Proteopedia
| 1rzw, 1 NMR models () | |||||||||
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| Gene: | AF2095 (Archaeoglobus fulgidus) | ||||||||
| Domains: | PTH2 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
The Solution Structure of the Archaeglobus fulgidis protein AF2095. Northeast Structural Genomics Consortium target GR4
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1RZW is a 1 chain structure of sequence from Archaeoglobus fulgidus. Full experimental information is available from OCA.
Reference
- 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. Solution structure of Archaeglobus fulgidis peptidyl-tRNA hydrolase (Pth2) provides evidence for an extensive conserved family of Pth2 enzymes in archea, bacteria, and eukaryotes. Protein Sci. 2005 Nov;14(11):2849-61. PMID:16251366
- Powers R, Acton TB, Chiang Y, Rajan PK, Cort JR, Kennedy MA, Liu J, Ma L, Rost B, Montelione GT. (1)H, (13)C and (15)N assignments for the Archaeglobus fulgidis protein AF2095. J Biomol NMR. 2004 Sep;30(1):107-8. PMID:15452442
Page seeded by OCA on Tue Feb 17 09:30:00 2009
Categories: Archaeoglobus fulgidus | 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-helice | Beta-sheet of 4 parallel | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi | Structural genomic
