1qxf

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(New page: 200px<br /><applet load="1qxf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qxf" /> '''SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN ...)
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'''SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S27E FROM ARCHAEOGLOBUS FULGIDUS: GR2, A NESG TARGET PROTEIN'''<br />
'''SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S27E FROM ARCHAEOGLOBUS FULGIDUS: GR2, A NESG TARGET PROTEIN'''<br />
==Overview==
==Overview==
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The Archaeoglobus fulgidis gene RS27_ARCFU encodes the 30S ribosomal, protein S27e. Here, we present the high-quality NMR solution structure of, this archaeal protein, which comprises a C4 zinc finger motif of the, CX(2)CX(14-16)CX(2)C class. S27e was selected as a target of the Northeast, Structural Genomics Consortium (target ID: GR2), and its three-dimensional, structure is the first representative of a family of more than 116, homologous proteins occurring in eukaryotic and archaeal cells. As a, salient feature of its molecular architecture, S27e exhibits a, beta-sandwich consisting of two three-stranded sheets with topology, B(decreasing), A(increasing), F(decreasing), and C(increasing), D(decreasing), E(increasing). Due to the uniqueness of the arrangement of, the strands, the resulting fold was found to be novel. Residues that are, highly conserved among the S27 proteins allowed identification of a, structural motif of putative functional importance; a conserved, hydrophobic patch may well play a pivotal role for functioning of S27, proteins, be it in archaeal or eukaryotic cells. The structure of human, S27, which possesses a 26-residue amino-terminal extension when compared, with the archaeal S27e, was modeled on the basis of two structural, templates, S27e for the carboxy-terminal core and the amino-terminal, segment of the archaeal ribosomal protein L37Ae for the extension., Remarkably, the electrostatic surface properties of archaeal and human, proteins are predicted to be entirely different, pointing at either, functional variations among archaeal and eukaryotic S27 proteins, or, assuming that the function remained invariant, to a concerted evolutionary, change of the surface potential of proteins interacting with S27.
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The Archaeoglobus fulgidis gene RS27_ARCFU encodes the 30S ribosomal protein S27e. Here, we present the high-quality NMR solution structure of this archaeal protein, which comprises a C4 zinc finger motif of the CX(2)CX(14-16)CX(2)C class. S27e was selected as a target of the Northeast Structural Genomics Consortium (target ID: GR2), and its three-dimensional structure is the first representative of a family of more than 116 homologous proteins occurring in eukaryotic and archaeal cells. As a salient feature of its molecular architecture, S27e exhibits a beta-sandwich consisting of two three-stranded sheets with topology B(decreasing), A(increasing), F(decreasing), and C(increasing), D(decreasing), E(increasing). Due to the uniqueness of the arrangement of the strands, the resulting fold was found to be novel. Residues that are highly conserved among the S27 proteins allowed identification of a structural motif of putative functional importance; a conserved hydrophobic patch may well play a pivotal role for functioning of S27 proteins, be it in archaeal or eukaryotic cells. The structure of human S27, which possesses a 26-residue amino-terminal extension when compared with the archaeal S27e, was modeled on the basis of two structural templates, S27e for the carboxy-terminal core and the amino-terminal segment of the archaeal ribosomal protein L37Ae for the extension. Remarkably, the electrostatic surface properties of archaeal and human proteins are predicted to be entirely different, pointing at either functional variations among archaeal and eukaryotic S27 proteins, or, assuming that the function remained invariant, to a concerted evolutionary change of the surface potential of proteins interacting with S27.
==About this Structure==
==About this Structure==
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1QXF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure superseeds the now removed PDB entry 1NVH. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QXF OCA].
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1QXF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure supersedes the now removed PDB entry 1NVH. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXF OCA].
==Reference==
==Reference==
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[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Acton, T.B.]]
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[[Category: Acton, T B.]]
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[[Category: Atreya, H.S.]]
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[[Category: Atreya, H S.]]
[[Category: Liu, G.]]
[[Category: Liu, G.]]
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[[Category: Montelione, G.T.]]
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[[Category: Montelione, G T.]]
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[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
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[[Category: NESG, Northeast Structural Genomics Consortium.]]
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[[Category: Penhoat, C.Herve.Du.]]
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[[Category: Penhoat, C Herve Du.]]
[[Category: Shen, Y.]]
[[Category: Shen, Y.]]
[[Category: Szyperski, T.]]
[[Category: Szyperski, T.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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Revision as of 12:44, 21 February 2008


1qxf

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SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S27E FROM ARCHAEOGLOBUS FULGIDUS: GR2, A NESG TARGET PROTEIN

Overview

The Archaeoglobus fulgidis gene RS27_ARCFU encodes the 30S ribosomal protein S27e. Here, we present the high-quality NMR solution structure of this archaeal protein, which comprises a C4 zinc finger motif of the CX(2)CX(14-16)CX(2)C class. S27e was selected as a target of the Northeast Structural Genomics Consortium (target ID: GR2), and its three-dimensional structure is the first representative of a family of more than 116 homologous proteins occurring in eukaryotic and archaeal cells. As a salient feature of its molecular architecture, S27e exhibits a beta-sandwich consisting of two three-stranded sheets with topology B(decreasing), A(increasing), F(decreasing), and C(increasing), D(decreasing), E(increasing). Due to the uniqueness of the arrangement of the strands, the resulting fold was found to be novel. Residues that are highly conserved among the S27 proteins allowed identification of a structural motif of putative functional importance; a conserved hydrophobic patch may well play a pivotal role for functioning of S27 proteins, be it in archaeal or eukaryotic cells. The structure of human S27, which possesses a 26-residue amino-terminal extension when compared with the archaeal S27e, was modeled on the basis of two structural templates, S27e for the carboxy-terminal core and the amino-terminal segment of the archaeal ribosomal protein L37Ae for the extension. Remarkably, the electrostatic surface properties of archaeal and human proteins are predicted to be entirely different, pointing at either functional variations among archaeal and eukaryotic S27 proteins, or, assuming that the function remained invariant, to a concerted evolutionary change of the surface potential of proteins interacting with S27.

About this Structure

1QXF is a Single protein structure of sequence from Archaeoglobus fulgidus. This structure supersedes the now removed PDB entry 1NVH. Full crystallographic information is available from OCA.

Reference

The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold., Herve du Penhoat C, Atreya HS, Shen Y, Liu G, Acton TB, Xiao R, Li Z, Murray D, Montelione GT, Szyperski T, Protein Sci. 2004 May;13(5):1407-16. PMID:15096641

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