1rzw
From Proteopedia
(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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'''The Solution Structure of the Archaeglobus fulgidis protein AF2095. Northeast Structural Genomics Consortium target GR4'''<br /> | '''The Solution Structure of the Archaeglobus fulgidis protein AF2095. Northeast Structural Genomics Consortium target GR4'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of protein AF2095 from the thermophilic archaea | + | 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== | ==About this Structure== | ||
| - | 1RZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http:// | + | 1RZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Acton, T | + | [[Category: Acton, T B.]] |
[[Category: Chiang, Y.]] | [[Category: Chiang, Y.]] | ||
| - | [[Category: Cort, J | + | [[Category: Cort, J R.]] |
| - | [[Category: Huang, Y | + | [[Category: Huang, Y J.]] |
| - | [[Category: Kennedy, M | + | [[Category: Kennedy, M A.]] |
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Ma, L.]] | [[Category: Ma, L.]] | ||
| - | [[Category: Montelione, G | + | [[Category: Montelione, G T.]] |
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: Powers, R.]] | [[Category: Powers, R.]] | ||
[[Category: Rost, B.]] | [[Category: Rost, B.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:25 2008'' |
Revision as of 12:56, 21 February 2008
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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 Thu Feb 21 14:56:25 2008
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
