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2iu1

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(New page: 200px<br /> <applet load="2iu1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iu1, resolution 1.80&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:2iu1.gif|left|200px]]<br />
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[[Image:2iu1.gif|left|200px]]<br /><applet load="2iu1" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2iu1" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2iu1, resolution 1.80&Aring;" />
caption="2iu1, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN'''<br />
'''CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN'''<br />
==Overview==
==Overview==
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The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5), plays a central role in the formation of the multifactor complex (MFC), an, important intermediate for the 43 S pre-initiation complex assembly. The, IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound, Met-tRNA(i)(Met) the MFC. In this work we present the high resolution, crystal structure of eIF5-CTD. This domain of the protein is exclusively, composed out of alpha-helices and is homologous to the carboxy-terminal, domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference, in the two structures is an additional carboxy-terminal helix in eIF5. The, binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure., eIF2-beta and eIF3 bind to non-overlapping patches of negative and, positive electrostatic potential, respectively.
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The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively.
==About this Structure==
==About this Structure==
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2IU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IU1 OCA].
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2IU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU1 OCA].
==Reference==
==Reference==
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[[Category: translation inititation]]
[[Category: translation inititation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:48:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:57 2008''

Revision as of 15:55, 21 February 2008


2iu1, resolution 1.80Å

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CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN

Overview

The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively.

About this Structure

2IU1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5., Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U, J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:16781736

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