2gil

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(New page: 200px<br /> <applet load="2gil" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gil, resolution 1.82&Aring;" /> '''Structure of the ex...)
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<applet load="2gil" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2gil, resolution 1.82&Aring;" />
caption="2gil, resolution 1.82&Aring;" />
'''Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 resolution'''<br />
'''Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 resolution'''<br />
==Overview==
==Overview==
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Rab/Ypt GTPases represent a&gt;60 member large family of membrane traffic, regulators in eukaryotic cells. Members of this group display intrinsic, GTPase activity varying over two orders of magnitude. Here, we show that, Rab6A represents the RabGTPase with the slowest spontaneous GTPase, activity yet measured (5x10(-6)s(-1)). Due to the very low intrinsic, hydrolysis rate we were able to crystallise and solve the structure of the, Rab6A:GTP complex to 1.82A resolution. Analysis of the structure suggests, that low catalytic activity of the Rab6A might be due to high flexibility, of the Switch II region and a low degree of constraint of critically, important for catalysis Gln 72.
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Rab/Ypt GTPases represent a&gt;60 member large family of membrane traffic regulators in eukaryotic cells. Members of this group display intrinsic GTPase activity varying over two orders of magnitude. Here, we show that Rab6A represents the RabGTPase with the slowest spontaneous GTPase activity yet measured (5x10(-6)s(-1)). Due to the very low intrinsic hydrolysis rate we were able to crystallise and solve the structure of the Rab6A:GTP complex to 1.82A resolution. Analysis of the structure suggests that low catalytic activity of the Rab6A might be due to high flexibility of the Switch II region and a low degree of constraint of critically important for catalysis Gln 72.
==About this Structure==
==About this Structure==
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2GIL 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 and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GIL OCA].
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2GIL 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> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GIL OCA].
==Reference==
==Reference==
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[[Category: protein-nucleotide complex]]
[[Category: protein-nucleotide complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:19:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:01 2008''

Revision as of 15:32, 21 February 2008


2gil, resolution 1.82Å

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Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 resolution

Overview

Rab/Ypt GTPases represent a>60 member large family of membrane traffic regulators in eukaryotic cells. Members of this group display intrinsic GTPase activity varying over two orders of magnitude. Here, we show that Rab6A represents the RabGTPase with the slowest spontaneous GTPase activity yet measured (5x10(-6)s(-1)). Due to the very low intrinsic hydrolysis rate we were able to crystallise and solve the structure of the Rab6A:GTP complex to 1.82A resolution. Analysis of the structure suggests that low catalytic activity of the Rab6A might be due to high flexibility of the Switch II region and a low degree of constraint of critically important for catalysis Gln 72.

About this Structure

2GIL is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A resolution., Bergbrede T, Pylypenko O, Rak A, Alexandrov K, J Struct Biol. 2005 Dec;152(3):235-8. Epub 2005 Nov 18. PMID:16332443

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