1bkb
From Proteopedia
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| - | [[Image:1bkb.jpg|left|200px]] | + | [[Image:1bkb.jpg|left|200px]] |
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| - | '''INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM''' | + | {{Structure |
| + | |PDB= 1bkb |SIZE=350|CAPTION= <scene name='initialview01'>1bkb</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BKB is a [ | + | 1BKB is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9753699 9753699] |
[[Category: Pyrobaculum aerophilum]] | [[Category: Pyrobaculum aerophilum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: translation initiation factor]] | [[Category: translation initiation factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:11 2008'' |
Revision as of 08:12, 20 March 2008
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| 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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