1nee

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(New page: 200px<br /><applet load="1nee" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nee" /> '''Structure of archaeal translation factor aIF...)
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[[Image:1nee.gif|left|200px]]<br /><applet load="1nee" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Structure of archaeal translation factor aIF2beta from Methanobacterium thermoautrophicum'''<br />
'''Structure of archaeal translation factor aIF2beta from Methanobacterium thermoautrophicum'''<br />
==Overview==
==Overview==
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aIF2 beta is the archaeal homolog of eIF2 beta, a member of the eIF2, heterotrimeric complex, implicated in the delivery of Met-tRNA(i)(Met) to, the 40S ribosomal subunit. We have determined the solution structure of, the intact beta-subunit of aIF2 from Methanobacterium thermoautotrophicum., aIF2 beta is composed of an unfolded N terminus, a mixed alpha/beta core, domain and a C-terminal zinc finger. NMR data shows the two folded domains, display restricted mobility with respect to each other. Analysis of the, aIF2 gamma structure docked to tRNA allowed the identification of a, putative binding site for the beta-subunit in the ternary translation, complex. Based on structural similarity and biochemical data, a role for, the different secondary structure elements is suggested.
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aIF2 beta is the archaeal homolog of eIF2 beta, a member of the eIF2 heterotrimeric complex, implicated in the delivery of Met-tRNA(i)(Met) to the 40S ribosomal subunit. We have determined the solution structure of the intact beta-subunit of aIF2 from Methanobacterium thermoautotrophicum. aIF2 beta is composed of an unfolded N terminus, a mixed alpha/beta core domain and a C-terminal zinc finger. NMR data shows the two folded domains display restricted mobility with respect to each other. Analysis of the aIF2 gamma structure docked to tRNA allowed the identification of a putative binding site for the beta-subunit in the ternary translation complex. Based on structural similarity and biochemical data, a role for the different secondary structure elements is suggested.
==About this Structure==
==About this Structure==
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1NEE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NEE OCA].
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1NEE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEE OCA].
==Reference==
==Reference==
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[[Category: Gutierrez, P.]]
[[Category: Gutierrez, P.]]
[[Category: Siddiqui, N.]]
[[Category: Siddiqui, N.]]
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[[Category: Trempe, J.F.]]
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[[Category: Trempe, J F.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: mixed alpha-beta structure]]
[[Category: mixed alpha-beta structure]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:11:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:13 2008''

Revision as of 12:05, 21 February 2008


1nee

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Structure of archaeal translation factor aIF2beta from Methanobacterium thermoautrophicum

Overview

aIF2 beta is the archaeal homolog of eIF2 beta, a member of the eIF2 heterotrimeric complex, implicated in the delivery of Met-tRNA(i)(Met) to the 40S ribosomal subunit. We have determined the solution structure of the intact beta-subunit of aIF2 from Methanobacterium thermoautotrophicum. aIF2 beta is composed of an unfolded N terminus, a mixed alpha/beta core domain and a C-terminal zinc finger. NMR data shows the two folded domains display restricted mobility with respect to each other. Analysis of the aIF2 gamma structure docked to tRNA allowed the identification of a putative binding site for the beta-subunit in the ternary translation complex. Based on structural similarity and biochemical data, a role for the different secondary structure elements is suggested.

About this Structure

1NEE is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the archaeal translation initiation factor aIF2 beta from Methanobacterium thermoautotrophicum: implications for translation initiation., Gutierrez P, Osborne MJ, Siddiqui N, Trempe JF, Arrowsmith C, Gehring K, Protein Sci. 2004 Mar;13(3):659-67. PMID:14978306

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