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<StructureSection load='1bkb' size='340' side='right'caption='[[1bkb]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='1bkb' size='340' side='right'caption='[[1bkb]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bkb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BKB FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bkb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BKB FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1bkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkb OCA], [https://pdbe.org/1bkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bkb RCSB], [https://www.ebi.ac.uk/pdbsum/1bkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bkb ProSAT]</span></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=1bkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkb OCA], [https://pdbe.org/1bkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bkb RCSB], [https://www.ebi.ac.uk/pdbsum/1bkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bkb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IF5A_PYRAE IF5A_PYRAE]] Functions by promoting the formation of the first peptide bond.  
[https://www.uniprot.org/uniprot/IF5A_PYRAE IF5A_PYRAE] Functions by promoting the formation of the first peptide bond.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=1bkb ConSurf].
</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=1bkb ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Translation initiation factor 5A (IF-5A) is reported to be involved in the first step of peptide bond formation in translation, to be involved in cell-cycle regulation and to be a cofactor for the Rev and Rex transactivator proteins of human immunodeficiency virus-1 and T-cell leukemia virus I, respectively. IF-5A contains an unusual amino acid, hypusine (N-epsilon-(4-aminobutyl-2-hydroxy)lysine), that is required for its function. The first step in the post-translational modification of lysine to hypusine is catalyzed by the enzyme deoxyhypusine synthase, the structure of which has been published recently. RESULTS: IF-5A from the archebacterium Pyrobaculum aerophilum has been heterologously expressed in Escherichia coli with selenomethionine substitution. The crystal structure of IF-5A has been determined by multiwavelength anomalous diffraction and refined to 1.75 A. Unmodified P. aerophilum IF-5A is found to be a beta structure with two domains and three separate hydrophobic cores. CONCLUSIONS: The lysine (Lys42) that is post-translationally modified by deoxyhypusine synthase is found at one end of the IF-5A molecule in an turn between beta strands beta4 and beta5; this lysine residue is freely solvent accessible. The C-terminal domain is found to be homologous to the cold-shock protein CspA of E. coli, which has a well characterized RNA-binding fold, suggesting that IF-5A is involved in RNA binding.
Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution.,Peat TS, Newman J, Waldo GS, Berendzen J, Terwilliger TC Structure. 1998 Sep 15;6(9):1207-14. PMID:9753699<ref>PMID:9753699</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bkb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Berendzen, J]]
[[Category: Pyrobaculum aerophilum]]
[[Category: Newman, J]]
[[Category: Berendzen J]]
[[Category: Peat, T S]]
[[Category: Newman J]]
[[Category: Terwilliger, T C]]
[[Category: Peat TS]]
[[Category: Waldo, G S]]
[[Category: Terwilliger TC]]
[[Category: Translation]]
[[Category: Waldo GS]]
[[Category: Translation initiation factor]]

Revision as of 15:33, 13 March 2024

INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM

1bkb, resolution 1.75Å

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