2aeu: Difference between revisions

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New page: left|200px<br /><applet load="2aeu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aeu, resolution 1.70Å" /> '''MJ0158, apo form'''<...
 
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[[Image:2aeu.gif|left|200px]]<br /><applet load="2aeu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2aeu, resolution 1.70&Aring;" />
'''MJ0158, apo form'''<br />


==Overview==
==MJ0158, apo form==
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.
<StructureSection load='2aeu' size='340' side='right'caption='[[2aeu]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2aeu]] 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=2AEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEU FirstGlance]. <br>
2AEU 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=2AEU OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aeu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aeu OCA], [https://pdbe.org/2aeu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aeu RCSB], [https://www.ebi.ac.uk/pdbsum/2aeu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aeu ProSAT]</span></td></tr>
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]
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y158_METJA Y158_METJA]
== 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/ae/2aeu_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=2aeu ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Engelhardt H]]
[[Category: Engelhardt, H.]]
[[Category: Gromadski K]]
[[Category: Gromadski, K.]]
[[Category: Kaiser JT]]
[[Category: Kaiser, J.T.]]
[[Category: Rodnina MV]]
[[Category: Rodnina, M.V.]]
[[Category: Rother M]]
[[Category: Rother, M.]]
[[Category: Wahl MC]]
[[Category: Wahl, M.C.]]
[[Category: SO4]]
[[Category: homo-oligomerization]]
[[Category: plp]]
[[Category: pyridoxal phosphate]]
[[Category: selenocysteine synthase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:05:14 2007''

Latest revision as of 16:40, 13 March 2024

MJ0158, apo formMJ0158, apo form

Structural highlights

2aeu is a 1 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Y158_METJA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

2aeu, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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