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2aev

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(New page: 200px<br /><applet load="2aev" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aev, resolution 2.00&Aring;" /> '''MJ0158, NaBH4-reduce...)
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[[Image:2aev.gif|left|200px]]<br /><applet load="2aev" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2aev, resolution 2.00&Aring;" />
 
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'''MJ0158, NaBH4-reduced form'''<br />
 
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==Overview==
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==MJ0158, NaBH4-reduced form==
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Bacterial selenocysteine synthase converts seryl-tRNA(Sec) to, selenocysteinyl-tRNA(Sec) for selenoprotein biosynthesis. The identity of, this enzyme in archaea and eukaryotes is unknown. On the basis of sequence, similarity, a conserved open reading frame has been annotated as a, selenocysteine synthase gene in archaeal genomes. We have determined the, crystal structure of the corresponding protein from Methanococcus, jannaschii, MJ0158. The protein was found to be dimeric with a distinctive, domain arrangement and an exposed active site, built from residues of the, large domain of one protomer alone. The shape of the dimer is reminiscent, of a substructure of the decameric Escherichia coli selenocysteine, synthase seen in electron microscopic projections. However, biochemical, analyses demonstrated that MJ0158 lacked affinity for E. coli, seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and neither substrate, was directly converted to selenocysteinyl-tRNA(Sec) by MJ0158 when, supplied with selenophosphate. We then tested a hypothetical M. jannaschii, O-phosphoseryl-tRNA(Sec) kinase and demonstrated that the enzyme converts, seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec) that could constitute an, activated intermediate for selenocysteinyl-tRNA(Sec) production. MJ0158, also failed to convert O-phosphoseryl-tRNA(Sec) to, selenocysteinyl-tRNA(Sec). In contrast, both archaeal and bacterial, seryl-tRNA synthetases were able to charge both archaeal and bacterial, tRNA(Sec) with serine, and E. coli selenocysteine synthase converted both, types of seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec). These findings, demonstrate that a number of factors from the selenoprotein biosynthesis, machineries are cross-reactive between the bacterial and the archaeal, systems but that MJ0158 either does not encode a selenocysteine synthase, or requires additional factors for activity.
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<StructureSection load='2aev' size='340' side='right'caption='[[2aev]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2aev]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEV FirstGlance]. <br>
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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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=2aev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aev OCA], [https://pdbe.org/2aev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aev RCSB], [https://www.ebi.ac.uk/pdbsum/2aev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aev ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Y158_METJA Y158_METJA]
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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/ae/2aev_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2aev 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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Bacterial selenocysteine synthase converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) for selenoprotein biosynthesis. The identity of this enzyme in archaea and eukaryotes is unknown. On the basis of sequence similarity, a conserved open reading frame has been annotated as a selenocysteine synthase gene in archaeal genomes. We have determined the crystal structure of the corresponding protein from Methanococcus jannaschii, MJ0158. The protein was found to be dimeric with a distinctive domain arrangement and an exposed active site, built from residues of the large domain of one protomer alone. The shape of the dimer is reminiscent of a substructure of the decameric Escherichia coli selenocysteine synthase seen in electron microscopic projections. However, biochemical analyses demonstrated that MJ0158 lacked affinity for E. coli seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and neither substrate was directly converted to selenocysteinyl-tRNA(Sec) by MJ0158 when supplied with selenophosphate. We then tested a hypothetical M. jannaschii O-phosphoseryl-tRNA(Sec) kinase and demonstrated that the enzyme converts seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec) that could constitute an activated intermediate for selenocysteinyl-tRNA(Sec) production. MJ0158 also failed to convert O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec). In contrast, both archaeal and bacterial seryl-tRNA synthetases were able to charge both archaeal and bacterial tRNA(Sec) with serine, and E. coli selenocysteine synthase converted both types of seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec). These findings demonstrate that a number of factors from the selenoprotein biosynthesis machineries are cross-reactive between the bacterial and the archaeal systems but that MJ0158 either does not encode a selenocysteine synthase or requires additional factors for activity.
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==About this Structure==
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Structural and functional investigation of a putative archaeal selenocysteine synthase.,Kaiser JT, Gromadski K, Rother M, Engelhardt H, Rodnina MV, Wahl MC Biochemistry. 2005 Oct 11;44(40):13315-27. PMID:16201757<ref>PMID:16201757</ref>
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2AEV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AEV OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural and functional investigation of a putative archaeal selenocysteine synthase., Kaiser JT, Gromadski K, Rother M, Engelhardt H, Rodnina MV, Wahl MC, Biochemistry. 2005 Oct 11;44(40):13315-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16201757 16201757]
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</div>
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<div class="pdbe-citations 2aev" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
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[[Category: Single protein]]
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[[Category: Engelhardt H]]
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[[Category: Engelhardt, H.]]
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[[Category: Gromadski K]]
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[[Category: Gromadski, K.]]
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[[Category: Kaiser JT]]
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[[Category: Kaiser, J.T.]]
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[[Category: Rodnina MV]]
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[[Category: Rodnina, M.V.]]
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[[Category: Rother M]]
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[[Category: Rother, M.]]
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[[Category: Wahl MC]]
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[[Category: Wahl, M.C.]]
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[[Category: SO4]]
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[[Category: homo-oligomerization]]
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[[Category: plp]]
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[[Category: pyridoxal phosphate]]
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[[Category: selenocysteine synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:05:17 2007''
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Current revision

MJ0158, NaBH4-reduced form

PDB ID 2aev

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