1mky

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(New page: 200px<br /><applet load="1mky" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mky, resolution 1.90&Aring;" /> '''Structural Analysis ...)
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[[Image:1mky.jpg|left|200px]]<br /><applet load="1mky" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mky, resolution 1.90&Aring;" />
caption="1mky, resolution 1.90&Aring;" />
'''Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains'''<br />
'''Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains'''<br />
==Overview==
==Overview==
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The EngA subfamily of essential bacterial GTPases has a unique domain, structure consisting of two adjacent GTPase domains (GD1 and GD2) and a, C-terminal domain. The structure of Thermotoga maritima Der bound to GDP, determined at 1.9 A resolution reveals a novel domain arrangement in which, the GTPase domains pack at either side of the C-terminal domain., Unexpectedly, the C-terminal domain resembles a KH domain, missing the, distinctive RNA recognition elements. Conserved motifs of the nucleotide, binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly, influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH, domain interface is distal to the GDP binding site of GD2.
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The EngA subfamily of essential bacterial GTPases has a unique domain structure consisting of two adjacent GTPase domains (GD1 and GD2) and a C-terminal domain. The structure of Thermotoga maritima Der bound to GDP determined at 1.9 A resolution reveals a novel domain arrangement in which the GTPase domains pack at either side of the C-terminal domain. Unexpectedly, the C-terminal domain resembles a KH domain, missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2.
==About this Structure==
==About this Structure==
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1MKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with PO4 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=1MKY OCA].
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1MKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=PO4:'>PO4</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=1MKY OCA].
==Reference==
==Reference==
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[[Category: Hwang, J.]]
[[Category: Hwang, J.]]
[[Category: Inouye, M.]]
[[Category: Inouye, M.]]
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[[Category: Robinson, V.L.]]
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[[Category: Robinson, V L.]]
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[[Category: Stock, A.M.]]
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[[Category: Stock, A M.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: tandem g-domains]]
[[Category: tandem g-domains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:29:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:19 2008''

Revision as of 11:56, 21 February 2008

Image:1mky.jpg

1mky, resolution 1.90Å

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Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains

Overview

The EngA subfamily of essential bacterial GTPases has a unique domain structure consisting of two adjacent GTPase domains (GD1 and GD2) and a C-terminal domain. The structure of Thermotoga maritima Der bound to GDP determined at 1.9 A resolution reveals a novel domain arrangement in which the GTPase domains pack at either side of the C-terminal domain. Unexpectedly, the C-terminal domain resembles a KH domain, missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2.

About this Structure

1MKY is a Single protein structure of sequence from Thermotoga maritima with and as ligands. Full crystallographic information is available from OCA.

Reference

Domain arrangement of Der, a switch protein containing two GTPase domains., Robinson VL, Hwang J, Fox E, Inouye M, Stock AM, Structure. 2002 Dec;10(12):1649-58. PMID:12467572

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