1bkb
From Proteopedia
(New page: 200px<br /><applet load="1bkb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bkb, resolution 1.75Å" /> '''INITIATION FACTOR 5A...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bkb.jpg|left|200px]]<br /><applet load="1bkb" size=" | + | [[Image:1bkb.jpg|left|200px]]<br /><applet load="1bkb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bkb, resolution 1.75Å" /> | caption="1bkb, resolution 1.75Å" /> | ||
'''INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM'''<br /> | '''INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Translation initiation factor 5A (IF-5A) is reported to be | + | 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== | ==About this Structure== | ||
| - | 1BKB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http:// | + | 1BKB is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 15: | Line 15: | ||
[[Category: Berendzen, J.]] | [[Category: Berendzen, J.]] | ||
[[Category: Newman, J.]] | [[Category: Newman, J.]] | ||
| - | [[Category: Peat, T | + | [[Category: Peat, T S.]] |
| - | [[Category: Terwilliger, T | + | [[Category: Terwilliger, T C.]] |
| - | [[Category: Waldo, G | + | [[Category: Waldo, G S.]] |
[[Category: translation initiation factor]] | [[Category: translation initiation factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:12 2008'' |
Revision as of 09:56, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 11:56:12 2008
