1k81: Difference between revisions

Revision as of 09:55, 2 July 2008

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File:1k81.png

Template:STRUCTURE 1k81

NMR Structure of the Zinc-Ribbon Domain within Translation Initiation Factor 2 Subunit betaNMR Structure of the Zinc-Ribbon Domain within Translation Initiation Factor 2 Subunit beta

Template:ABSTRACT PUBMED 11980477

About this StructureAbout this Structure

1K81 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full experimental information is available from OCA.

ReferenceReference

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

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 {{STRUCTURE_1k81|  PDB=1k81  |  SCENE=  }}
-'''NMR Structure of the Zinc-Ribbon Domain within Translation Initiation Factor 2 Subunit beta'''
+===NMR Structure of the Zinc-Ribbon Domain within Translation Initiation Factor 2 Subunit beta===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11980477}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11980477 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11980477}}
 ==About this Structure==
-K81 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K81 OCA].
+K81 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K81 OCA].
 ==Reference==
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 [[Category: Translation initiation factor]]
 [[Category: Zinc ribbon]]
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