1ek0

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(New page: 200px<br /><applet load="1ek0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ek0, resolution 1.48&Aring;" /> '''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"
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[[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==
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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.
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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==
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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].
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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.]]
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[[Category: Scheidig, A.J.]]
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[[Category: Scheidig, A J.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: GNP]]
[[Category: GNP]]
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[[Category: ypt/rab protein]]
[[Category: ypt/rab protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:04:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:34 2008''

Revision as of 10:28, 21 February 2008


1ek0, resolution 1.48Å

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GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION

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.

About this Structure

1EK0 is a Single protein structure of sequence from Saccharomyces cerevisiae with , , and as ligands. Full crystallographic information is available from OCA.

Reference

High-resolution crystal structure of S. cerevisiae Ypt51(DeltaC15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis., Esters H, Alexandrov K, Constantinescu AT, Goody RS, Scheidig AJ, J Mol Biol. 2000 Apr 21;298(1):111-21. PMID:10756108

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