2hjg

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(New page: 200px<br /><applet load="2hjg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hjg, resolution 2.50&Aring;" /> '''The crystal structur...)
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[[Image:2hjg.gif|left|200px]]<br /><applet load="2hjg" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hjg.gif|left|200px]]<br /><applet load="2hjg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hjg, resolution 2.50&Aring;" />
caption="2hjg, resolution 2.50&Aring;" />
'''The crystal structure of the B. subtilis YphC GTPase in complex with GDP'''<br />
'''The crystal structure of the B. subtilis YphC GTPase in complex with GDP'''<br />
==Overview==
==Overview==
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The structure of a Bacillus subtilis YphC/GDP complex shows that it, contains two GTPase domains that pack against a central domain whose fold, resembles that of an RNA binding KH-domain. Comparisons of this structure, to that of a homologue in Thermotoga maritima reveals a dramatic, rearrangement in the position of the N-terminal GTPase domain with a shift, of up to 60 A and the formation of a totally different interface to the, central domain. This rearrangement appears to be triggered by, conformational changes of the switch II region in this domain in response, to nucleotide binding. Modeling studies suggest that this motion, represents transitions between the "on" and "off" states of the GTPase, the effect of which is to alternately expose and bury a positively charged, face of the central domain that we suggest is involved in RNA recognition, as part of the possible role of this enzyme in ribosome binding.
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The structure of a Bacillus subtilis YphC/GDP complex shows that it contains two GTPase domains that pack against a central domain whose fold resembles that of an RNA binding KH-domain. Comparisons of this structure to that of a homologue in Thermotoga maritima reveals a dramatic rearrangement in the position of the N-terminal GTPase domain with a shift of up to 60 A and the formation of a totally different interface to the central domain. This rearrangement appears to be triggered by conformational changes of the switch II region in this domain in response to nucleotide binding. Modeling studies suggest that this motion represents transitions between the "on" and "off" states of the GTPase, the effect of which is to alternately expose and bury a positively charged face of the central domain that we suggest is involved in RNA recognition as part of the possible role of this enzyme in ribosome binding.
==About this Structure==
==About this Structure==
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2HJG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN 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=2HJG OCA].
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2HJG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</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=2HJG OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Muench, S.P.]]
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[[Category: Muench, S P.]]
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[[Category: Rice, D.W]]
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[[Category: Rice, D W]]
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[[Category: Sedelnikova, S.E.]]
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[[Category: Sedelnikova, S E.]]
[[Category: Xu, L.]]
[[Category: Xu, L.]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: gtpase enga kh-domain]]
[[Category: gtpase enga kh-domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:48:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:35 2008''

Revision as of 15:42, 21 February 2008


2hjg, resolution 2.50Å

Drag the structure with the mouse to rotate

The crystal structure of the B. subtilis YphC GTPase in complex with GDP

Overview

The structure of a Bacillus subtilis YphC/GDP complex shows that it contains two GTPase domains that pack against a central domain whose fold resembles that of an RNA binding KH-domain. Comparisons of this structure to that of a homologue in Thermotoga maritima reveals a dramatic rearrangement in the position of the N-terminal GTPase domain with a shift of up to 60 A and the formation of a totally different interface to the central domain. This rearrangement appears to be triggered by conformational changes of the switch II region in this domain in response to nucleotide binding. Modeling studies suggest that this motion represents transitions between the "on" and "off" states of the GTPase, the effect of which is to alternately expose and bury a positively charged face of the central domain that we suggest is involved in RNA recognition as part of the possible role of this enzyme in ribosome binding.

About this Structure

2HJG is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Full crystallographic information is available from OCA.

Reference

The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding., Muench SP, Xu L, Sedelnikova SE, Rice DW, Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12359-64. Epub 2006 Aug 7. PMID:16894162

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