1ky3: Difference between revisions
New page: left|200px<br /><applet load="1ky3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ky3, resolution 1.35Å" /> '''GDP-BOUND YPT7P AT 1... |
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[[Image:1ky3.jpg|left|200px]]<br /><applet load="1ky3" size=" | [[Image:1ky3.jpg|left|200px]]<br /><applet load="1ky3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ky3, resolution 1.35Å" /> | caption="1ky3, resolution 1.35Å" /> | ||
'''GDP-BOUND YPT7P AT 1.35 A RESOLUTION'''<br /> | '''GDP-BOUND YPT7P AT 1.35 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The GTPase Ypt7p from S. cerevisiae is involved in late | The GTPase Ypt7p from S. cerevisiae is involved in late endosome-to-vacuole transport and homotypic vacuole fusion. We present crystal structures of the GDP- and GppNHp-bound conformation of Ypt7p solved at 1.35 and 1.6 A resolution, respectively. Despite the similarity of the overall structure to other Ypt/Rab proteins, Ypt7p displays small but significant differences. The Ypt7p-specific residues Tyr33 and Tyr37 cause a difference in the main chain trace of the RabSF2 region and form a characteristic surface epitope. Ypt7p*GppNHp does not display the helix alpha2, characteristic of the Ras-superfamily, but instead possess an extended loop L4/L5. Due to insertions in loops L3 and L7, the neighboring RabSF1 and RabSF4 regions are different in their conformations to those of other Ypt/Rab proteins. | ||
==About this Structure== | ==About this Structure== | ||
1KY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1KY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] 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=1KY3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Constantinescu, A | [[Category: Constantinescu, A T.]] | ||
[[Category: Rak, A.]] | [[Category: Rak, A.]] | ||
[[Category: Scheidig, A | [[Category: Scheidig, A J.]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: ypt/rab protein]] | [[Category: ypt/rab protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:11 2008'' | ||
Revision as of 14:39, 21 February 2008
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GDP-BOUND YPT7P AT 1.35 A RESOLUTION
OverviewOverview
The GTPase Ypt7p from S. cerevisiae is involved in late endosome-to-vacuole transport and homotypic vacuole fusion. We present crystal structures of the GDP- and GppNHp-bound conformation of Ypt7p solved at 1.35 and 1.6 A resolution, respectively. Despite the similarity of the overall structure to other Ypt/Rab proteins, Ypt7p displays small but significant differences. The Ypt7p-specific residues Tyr33 and Tyr37 cause a difference in the main chain trace of the RabSF2 region and form a characteristic surface epitope. Ypt7p*GppNHp does not display the helix alpha2, characteristic of the Ras-superfamily, but instead possess an extended loop L4/L5. Due to insertions in loops L3 and L7, the neighboring RabSF1 and RabSF4 regions are different in their conformations to those of other Ypt/Rab proteins.
About this StructureAbout this Structure
1KY3 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases., Constantinescu AT, Rak A, Alexandrov K, Esters H, Goody RS, Scheidig AJ, Structure. 2002 Apr;10(4):569-79. PMID:11937061
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