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1r2q

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(New page: 200px<br /> <applet load="1r2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2q, resolution 1.05&Aring;" /> '''Crystal Structure o...)
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<applet load="1r2q" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1r2q, resolution 1.05&Aring;" />
caption="1r2q, resolution 1.05&Aring;" />
'''Crystal Structure of Human Rab5a GTPase Domain at 1.05 A resolution'''<br />
'''Crystal Structure of Human Rab5a GTPase Domain at 1.05 A resolution'''<br />
==Overview==
==Overview==
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Rab5 is a GTPase that regulates early endosome fusion. Its GTPase domain, crystal structure is reported here at 1.05 A resolution in complex with a, GTP-analog molecule. It provides the highest resolution three-dimensional, model so far obtained for proteins from the Ras-like GTPase family. This, study allows extension of structural examination of the GTPase machinery, as well as of high-resolution protein structures in general. For example, a buried water-molecule network was observed underneath the switch, regions, which is consistent with the functional roles of these regions in, the molecular-switching process. Furthermore, residues of multiple, conformation and clustered distribution of anisotropic thermal motions of, the protein molecule may have general implications for the function of, Ras-like GTPases.
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Rab5 is a GTPase that regulates early endosome fusion. Its GTPase domain crystal structure is reported here at 1.05 A resolution in complex with a GTP-analog molecule. It provides the highest resolution three-dimensional model so far obtained for proteins from the Ras-like GTPase family. This study allows extension of structural examination of the GTPase machinery as well as of high-resolution protein structures in general. For example, a buried water-molecule network was observed underneath the switch regions, which is consistent with the functional roles of these regions in the molecular-switching process. Furthermore, residues of multiple conformation and clustered distribution of anisotropic thermal motions of the protein molecule may have general implications for the function of Ras-like GTPases.
==About this Structure==
==About this Structure==
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1R2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, GNP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R2Q OCA].
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1R2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GNP:'>GNP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2Q OCA].
==Reference==
==Reference==
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[[Category: Li, G.]]
[[Category: Li, G.]]
[[Category: Terzyan, S.]]
[[Category: Terzyan, S.]]
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[[Category: Zhang, X.C.]]
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[[Category: Zhang, X C.]]
[[Category: Zhu, G.]]
[[Category: Zhu, G.]]
[[Category: GNP]]
[[Category: GNP]]
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[[Category: rab]]
[[Category: rab]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:59:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:25 2008''

Revision as of 12:46, 21 February 2008


1r2q, resolution 1.05Å

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Crystal Structure of Human Rab5a GTPase Domain at 1.05 A resolution

Overview

Rab5 is a GTPase that regulates early endosome fusion. Its GTPase domain crystal structure is reported here at 1.05 A resolution in complex with a GTP-analog molecule. It provides the highest resolution three-dimensional model so far obtained for proteins from the Ras-like GTPase family. This study allows extension of structural examination of the GTPase machinery as well as of high-resolution protein structures in general. For example, a buried water-molecule network was observed underneath the switch regions, which is consistent with the functional roles of these regions in the molecular-switching process. Furthermore, residues of multiple conformation and clustered distribution of anisotropic thermal motions of the protein molecule may have general implications for the function of Ras-like GTPases.

About this Structure

1R2Q is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution., Terzyan S, Zhu G, Li G, Zhang XC, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):54-60. Epub 2003, Dec 18. PMID:14684892

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