1yzn
From Proteopedia
(New page: 200px<br /><applet load="1yzn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yzn, resolution 2.06Å" /> '''GppNHp-Bound Ypt1p G...) |
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| - | [[Image:1yzn.gif|left|200px]]<br /><applet load="1yzn" size=" | + | [[Image:1yzn.gif|left|200px]]<br /><applet load="1yzn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yzn, resolution 2.06Å" /> | caption="1yzn, resolution 2.06Å" /> | ||
'''GppNHp-Bound Ypt1p GTPase'''<br /> | '''GppNHp-Bound Ypt1p GTPase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rab GTPases regulate all stages of membrane trafficking, including vesicle | + | Rab GTPases regulate all stages of membrane trafficking, including vesicle budding, cargo sorting, transport, tethering and fusion. In the inactive (GDP-bound) conformation, accessory factors facilitate the targeting of Rab GTPases to intracellular compartments. After nucleotide exchange to the active (GTP-bound) conformation, Rab GTPases interact with functionally diverse effectors including lipid kinases, motor proteins and tethering complexes. How effectors distinguish between homologous Rab GTPases represents an unresolved problem with respect to the specificity of vesicular trafficking. Using a structural proteomic approach, we have determined the specificity and structural basis underlying the interaction of the multivalent effector rabenosyn-5 with the Rab family. The results demonstrate that even the structurally similar effector domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions. The observed specificity is determined at a family-wide level by structural diversity in the active conformation, which governs the spatial disposition of critical conserved recognition determinants, and by a small number of both positive and negative sequence determinants that allow further discrimination between Rab GTPases with similar switch conformations. |
==About this Structure== | ==About this Structure== | ||
| - | 1YZN 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 GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YZN 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=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Eathiraj, S.]] | [[Category: Eathiraj, S.]] | ||
| - | [[Category: Lambright, D | + | [[Category: Lambright, D G.]] |
[[Category: Pan, X.]] | [[Category: Pan, X.]] | ||
[[Category: Ritacco, C.]] | [[Category: Ritacco, C.]] | ||
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[[Category: ypt1p gtpase]] | [[Category: ypt1p gtpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:42 2008'' |
Revision as of 14:10, 21 February 2008
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GppNHp-Bound Ypt1p GTPase
Overview
Rab GTPases regulate all stages of membrane trafficking, including vesicle budding, cargo sorting, transport, tethering and fusion. In the inactive (GDP-bound) conformation, accessory factors facilitate the targeting of Rab GTPases to intracellular compartments. After nucleotide exchange to the active (GTP-bound) conformation, Rab GTPases interact with functionally diverse effectors including lipid kinases, motor proteins and tethering complexes. How effectors distinguish between homologous Rab GTPases represents an unresolved problem with respect to the specificity of vesicular trafficking. Using a structural proteomic approach, we have determined the specificity and structural basis underlying the interaction of the multivalent effector rabenosyn-5 with the Rab family. The results demonstrate that even the structurally similar effector domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions. The observed specificity is determined at a family-wide level by structural diversity in the active conformation, which governs the spatial disposition of critical conserved recognition determinants, and by a small number of both positive and negative sequence determinants that allow further discrimination between Rab GTPases with similar switch conformations.
About this Structure
1YZN is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of family-wide Rab GTPase recognition by rabenosyn-5., Eathiraj S, Pan X, Ritacco C, Lambright DG, Nature. 2005 Jul 21;436(7049):415-9. PMID:16034420
Page seeded by OCA on Thu Feb 21 16:10:42 2008
