1d2e

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(New page: 200px<br /><applet load="1d2e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d2e, resolution 1.94&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1d2e.jpg|left|200px]]<br /><applet load="1d2e" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1d2e, resolution 1.94&Aring;" />
caption="1d2e, resolution 1.94&Aring;" />
'''CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP'''<br />
'''CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP'''<br />
==Overview==
==Overview==
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The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu), in complex with GDP has been determined at a resolution of 1. 94 A. The, structure is similar to that of EF-Tu:GDP from Escherichia coli and, Thermus aquaticus, but the orientation of the GDP-binding domain 1 is, changed relative to domains 2 and 3. Sixteen conserved water molecules, common to EF-Tu and other G-proteins in the GDP-binding site are, described. These water molecules create a network linking separated parts, of the binding pocket. Mitochondrial EF-Tu binds nucleotides less tightly, than prokaryotic EF-Tu possibly due to an increased mobility in regions, close to the GDP-binding site. The C-terminal extension of mitochondrial, EF-Tu has structural similarities with DNA recognising zinc fingers, suggesting that the extension may be involved in recognition of RNA.
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The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu) in complex with GDP has been determined at a resolution of 1. 94 A. The structure is similar to that of EF-Tu:GDP from Escherichia coli and Thermus aquaticus, but the orientation of the GDP-binding domain 1 is changed relative to domains 2 and 3. Sixteen conserved water molecules common to EF-Tu and other G-proteins in the GDP-binding site are described. These water molecules create a network linking separated parts of the binding pocket. Mitochondrial EF-Tu binds nucleotides less tightly than prokaryotic EF-Tu possibly due to an increased mobility in regions close to the GDP-binding site. The C-terminal extension of mitochondrial EF-Tu has structural similarities with DNA recognising zinc fingers suggesting that the extension may be involved in recognition of RNA.
==About this Structure==
==About this Structure==
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1D2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D2E OCA].
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1D2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2E OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Andersen, G.R.]]
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[[Category: Andersen, G R.]]
[[Category: Nyborg, J.]]
[[Category: Nyborg, J.]]
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[[Category: Spremulli, L.L.]]
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[[Category: Spremulli, L L.]]
[[Category: Thirup, S.]]
[[Category: Thirup, S.]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: g-protein]]
[[Category: g-protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:57:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:15 2008''

Revision as of 10:12, 21 February 2008

Image:1d2e.jpg

1d2e, resolution 1.94Å

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CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP

Overview

The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu) in complex with GDP has been determined at a resolution of 1. 94 A. The structure is similar to that of EF-Tu:GDP from Escherichia coli and Thermus aquaticus, but the orientation of the GDP-binding domain 1 is changed relative to domains 2 and 3. Sixteen conserved water molecules common to EF-Tu and other G-proteins in the GDP-binding site are described. These water molecules create a network linking separated parts of the binding pocket. Mitochondrial EF-Tu binds nucleotides less tightly than prokaryotic EF-Tu possibly due to an increased mobility in regions close to the GDP-binding site. The C-terminal extension of mitochondrial EF-Tu has structural similarities with DNA recognising zinc fingers suggesting that the extension may be involved in recognition of RNA.

About this Structure

1D2E is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.

Reference

High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP., Andersen GR, Thirup S, Spremulli LL, Nyborg J, J Mol Biol. 2000 Mar 24;297(2):421-36. PMID:10715211

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