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New page: left|200px<br /><applet load="1ek0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ek0, resolution 1.48Å" /> '''GPPNHP-BOUND YPT51 A...
 
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[[Image:1ek0.jpg|left|200px]]<br /><applet load="1ek0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ek0.jpg|left|200px]]<br /><applet load="1ek0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ek0, resolution 1.48&Aring;" />
caption="1ek0, resolution 1.48&Aring;" />
'''GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION'''<br />
'''GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION'''<br />


==Overview==
==Overview==
Ypt/Rab proteins are membrane-associated small GTP-binding proteins which, play a central role in the coordination, activation and regulation of, vesicle-mediated transport in eukaryotic cells. We present the 1.5 A, high-resolution crystal structure of Ypt51 in its active, GppNHp-bound, conformation. Ypt51 is an important regulator involved in the endocytic, membrane traffic of Saccharomyces cerevisiae. The structure reveals small, but significant structural differences compared with H-Ras p21. The, effector loop and the catalytic loop are well defined and stabilized by, extensive hydrophobic interactions. The switch I and switch II regions, form a well-defined epitope for hypothetical effector protein binding., Sequence comparisons between the different isoforms Ypt51, Ypt52 and Ypt53, provide the first insights into determinants for specific effector binding, and for fine-tuning of the intrinsic GTP-hydrolysis rate.
Ypt/Rab proteins are membrane-associated small GTP-binding proteins which play a central role in the coordination, activation and regulation of vesicle-mediated transport in eukaryotic cells. We present the 1.5 A high-resolution crystal structure of Ypt51 in its active, GppNHp-bound conformation. Ypt51 is an important regulator involved in the endocytic membrane traffic of Saccharomyces cerevisiae. The structure reveals small but significant structural differences compared with H-Ras p21. The effector loop and the catalytic loop are well defined and stabilized by extensive hydrophobic interactions. The switch I and switch II regions form a well-defined epitope for hypothetical effector protein binding. Sequence comparisons between the different isoforms Ypt51, Ypt52 and Ypt53 provide the first insights into determinants for specific effector binding and for fine-tuning of the intrinsic GTP-hydrolysis rate.


==About this Structure==
==About this Structure==
1EK0 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, NI, GNP 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=1EK0 OCA].  
1EK0 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>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=GNP:'>GNP</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=1EK0 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Esters, H.]]
[[Category: Esters, H.]]
[[Category: Scheidig, A.J.]]
[[Category: Scheidig, A J.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: GNP]]
[[Category: GNP]]
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[[Category: ypt/rab protein]]
[[Category: ypt/rab protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:04:15 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:34 2008''