1bkb
From Proteopedia
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|PDB= 1bkb |SIZE=350|CAPTION= <scene name='initialview01'>1bkb</scene>, resolution 1.75Å | |PDB= 1bkb |SIZE=350|CAPTION= <scene name='initialview01'>1bkb</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkb OCA], [http://www.ebi.ac.uk/pdbsum/1bkb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bkb RCSB]</span> | ||
}} | }} | ||
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[[Category: translation initiation factor]] | [[Category: translation initiation factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:02:52 2008'' |
Revision as of 16:02, 30 March 2008
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| , resolution 1.75Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM
Overview
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.
About this Structure
1BKB is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.
Reference
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
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