1k8b: Difference between revisions

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 ==NMR Structure Analysis of the N-terminal Domain of Archaeal Translation Initiation Factor 2 Subunit beta==
-<StructureSection load='1k8b' size='340' side='right'caption='[[1k8b]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1k8b' size='340' side='right'caption='[[1k8b]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1k8b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K8B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1k8b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K8B FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k81|1k81]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k8b OCA], [https://pdbe.org/1k8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k8b RCSB], [https://www.ebi.ac.uk/pdbsum/1k8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k8b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/IF2B_METJA IF2B_METJA]] eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (By similarity).
+[https://www.uniprot.org/uniprot/IF2B_METJA IF2B_METJA] eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1k8b ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The beta subunit of archaeal translation initiation factor 2 (aIF2beta) is a representative of a family of proteins whose members include the beta subunit of eukaryotic translation initiation factor 2 (eIF2beta) and the N-terminal domain within translation initiation factor 5 (eIF5); no members of this family of proteins have been structurally characterized up to this time. In the work presented here, aIF2beta from Methanococcus jannaschii was expressed in Escherichia coli, purified, and analyzed using multidimensional NMR methods. The aIF2beta was found to contain two independent structural domains. The N-terminal domain contains a four-stranded antiparallel beta sheet and two alpha helices, and is structurally similar to the DNA-binding domain of a yeast heat shock transcription factor and a domain within ribosomal protein S4. This structural similarity was an unanticipated result, since no significant homology was detected at the level of primary sequence. The C-terminal domain of aIF2beta contains a zinc-binding motif of three antiparallel beta strands, with four conserved cysteines arranged as two CXXC units separated by 17 residues. Conserved residues on the surface of each domain that are likely candidates for direct interaction with other components of the translational apparatus were identified. The significant primary sequence homology between archaeal aIF2beta and the eukaryotic eIF2beta and eIF5, when combined with the structural results in the work presented here, permitted structural features to be predicted for these latter two eukaryotic proteins.
-Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2beta/eIF5 family of proteins.,Cho S, Hoffman DW Biochemistry. 2002 May 7;41(18):5730-42. PMID:11980477<ref>PMID:11980477</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1k8b" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43067]]
 [[Category: Large Structures]]
-[[Category: Cho, S]]
+[[Category: Methanocaldococcus jannaschii]]
-[[Category: Hoffman, D W]]
+[[Category: Cho S]]
-[[Category: Aif2 subunit beta]]
+[[Category: Hoffman DW]]
-[[Category: N-terminal domain]]
-[[Category: Translation]]