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| - | [[Image:1qxf.gif|left|200px]] | |
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| - | {{Structure
| + | ==SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S27E FROM ARCHAEOGLOBUS FULGIDUS: GR2, A NESG TARGET PROTEIN== |
| - | |PDB= 1qxf |SIZE=350|CAPTION= <scene name='initialview01'>1qxf</scene>
| + | <StructureSection load='1qxf' size='340' side='right'caption='[[1qxf]]' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1qxf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nvh 1nvh]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QXF FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | |GENE=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxf OCA], [https://pdbe.org/1qxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qxf RCSB], [https://www.ebi.ac.uk/pdbsum/1qxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qxf ProSAT], [https://www.topsan.org/Proteins/NESGC/1qxf TOPSAN]</span></td></tr> |
| - | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00415 rps27e]</span>
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxf OCA], [http://www.ebi.ac.uk/pdbsum/1qxf PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1qxf RCSB]</span> | + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/RS27_ARCFU RS27_ARCFU] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/1qxf_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qxf ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | 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. |
| | | | |
| - | '''SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S27E FROM ARCHAEOGLOBUS FULGIDUS: GR2, A NESG TARGET PROTEIN'''
| + | 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<ref>PMID:15096641</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 1qxf" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | 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.
| + | *[[Ribosomal protein S27|Ribosomal protein S27]] |
| - | | + | == References == |
| - | ==About this Structure== | + | <references/> |
| - | 1QXF is a [[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].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/15096641 15096641]
| + | |
| | [[Category: Archaeoglobus fulgidus]] | | [[Category: Archaeoglobus fulgidus]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Acton, T B.]] | + | [[Category: Acton TB]] |
| - | [[Category: Atreya, H S.]] | + | [[Category: Atreya HS]] |
| - | [[Category: Liu, G.]] | + | [[Category: Herve Du Penhoat C]] |
| - | [[Category: Montelione, G T.]] | + | [[Category: Liu G]] |
| - | [[Category: NESG, Northeast Structural Genomics Consortium.]] | + | [[Category: Montelione GT]] |
| - | [[Category: Penhoat, C Herve Du.]]
| + | [[Category: Shen Y]] |
| - | [[Category: Shen, Y.]] | + | [[Category: Szyperski T]] |
| - | [[Category: Szyperski, T.]] | + | [[Category: Xiao R]] |
| - | [[Category: Xiao, R.]] | + | |
| - | [[Category: beta sheet]]
| + | |
| - | [[Category: nesg]]
| + | |
| - | [[Category: northeast structural genomics consortium]]
| + | |
| - | [[Category: protein structure initiative]]
| + | |
| - | [[Category: psi]]
| + | |
| - | [[Category: structural genomic]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:02:15 2008''
| + | |
| Structural highlights
Function
RS27_ARCFU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Herve du Penhoat C, Atreya HS, Shen Y, Liu G, Acton TB, Xiao R, Li Z, Murray D, Montelione GT, Szyperski T. The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold. Protein Sci. 2004 May;13(5):1407-16. PMID:15096641 doi:10.1110/ps.03589204
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