1q46

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[[Image:1q46.gif|left|200px]]
 
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==crystal structure of the eIF2 alpha subunit from saccharomyces cerevisia==
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The line below this paragraph, containing "STRUCTURE_1q46", creates the "Structure Box" on the page.
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<StructureSection load='1q46' size='340' side='right'caption='[[1q46]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1q46]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q46 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]] 2.86&#8491;</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=1q46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q46 OCA], [https://pdbe.org/1q46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q46 RCSB], [https://www.ebi.ac.uk/pdbsum/1q46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q46 ProSAT]</span></td></tr>
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{{STRUCTURE_1q46| PDB=1q46 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IF2A_YEAST IF2A_YEAST] eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
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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/q4/1q46_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=1q46 ConSurf].
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<div style="clear:both"></div>
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'''crystal structure of the eIF2 alpha subunit from saccharomyces cerevisia'''
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==See Also==
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*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The alpha subunit of translation initiation factor 2 (eIF2alpha) is the target of specific kinases that can phosphorylate a conserved serine residue as part of a mechanism for regulating protein expression at the translational level in eukaryotes. The structure of the 20 kDa N-terminal region of eIF2alpha from Saccharomyces cerevisiae was determined by X-ray crystallography at 2.5A resolution. In most respects, the structure is similar to that of the recently solved human eIF2alpha; the rather elongated protein contains a five-stranded antiparallel beta-barrel in its N-terminal region, followed by an almost entirely helical domain. The S.cerevisiae eIF2alpha lacks a disulfide bridge that is present in the homologous protein in humans and some of the other higher eukaryotes. Interestingly, a conserved loop consisting of residues 51-65 and containing serine 51, the putative phosphorylation site, is visible in the electron density maps of the S.cerevisiae eIF2alpha; most of this functionally important loop was not observed in the crystal structure of the human protein. This loop is relatively exposed to solvent, and contains two short 3(10) helices in addition to some extended structure. Serine 51 is located at the C-terminal end of one of the 3(10) helices and near several conserved positively charged residues. The side-chain of serine 51 is sufficiently exposed so that its phosphorylation would not necessitate a substantial change in the protein structure. The structures and relative positions of residues that have been implicated in kinase binding and in the interaction with guanine nucleotide exchange factor (eIF2B) are described.
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[[Category: Large Structures]]
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==About this Structure==
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1Q46 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q46 OCA].
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==Reference==
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The crystal structure of the N-terminal region of the alpha subunit of translation initiation factor 2 (eIF2alpha) from Saccharomyces cerevisiae provides a view of the loop containing serine 51, the target of the eIF2alpha-specific kinases., Dhaliwal S, Hoffman DW, J Mol Biol. 2003 Nov 21;334(2):187-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14607111 14607111]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Dhaliwal S]]
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[[Category: Dhaliwal, S.]]
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[[Category: Hoffman DW]]
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[[Category: Hoffman, D W.]]
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[[Category: Eif2]]
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[[Category: Initiation factor]]
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[[Category: Phosphorylation site]]
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[[Category: Translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:50:54 2008''
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Current revision

crystal structure of the eIF2 alpha subunit from saccharomyces cerevisia

PDB ID 1q46

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