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1lva

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[[Image:1lva.gif|left|200px]]
 
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{{Structure
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==Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB==
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|PDB= 1lva |SIZE=350|CAPTION= <scene name='initialview01'>1lva</scene>, resolution 2.12&Aring;
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<StructureSection load='1lva' size='340' side='right'caption='[[1lva]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=Y1:YTTRIUM+ION'>Y1</scene>
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<table><tr><td colspan='2'>[[1lva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LVA FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12&#8491;</td></tr>
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|GENE= SelB(amino acids 370-634) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1525 Moorella thermoacetica])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=Y1:YTTRIUM+ION'>Y1</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lva OCA], [https://pdbe.org/1lva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lva RCSB], [https://www.ebi.ac.uk/pdbsum/1lva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lva ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lva OCA], [http://www.ebi.ac.uk/pdbsum/1lva PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lva RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/SELB_MOOTH SELB_MOOTH] Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lv/1lva_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1lva ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Structural observations and data in the literature suggest that this change happens upon mRNA binding.
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'''Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB'''
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Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.,Selmer M, Su XD EMBO J. 2002 Aug 1;21(15):4145-53. PMID:12145214<ref>PMID:12145214</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1lva" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Structural observations and data in the literature suggest that this change happens upon mRNA binding.
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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*[[SelB|SelB]]
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==About this Structure==
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== References ==
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1LVA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVA OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB., Selmer M, Su XD, EMBO J. 2002 Aug 1;21(15):4145-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12145214 12145214]
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[[Category: Large Structures]]
[[Category: Moorella thermoacetica]]
[[Category: Moorella thermoacetica]]
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[[Category: Single protein]]
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[[Category: Selmer M]]
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[[Category: Selmer, M.]]
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[[Category: Su X-D]]
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[[Category: Su, X D.]]
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[[Category: winged-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:47 2008''
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Current revision

Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB

PDB ID 1lva

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