1u8y: Difference between revisions

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New page: left|200px<br /><applet load="1u8y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u8y, resolution 1.55Å" /> '''CRystal structures o...
 
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[[Image:1u8y.jpg|left|200px]]<br /><applet load="1u8y" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1u8y.jpg|left|200px]]<br /><applet load="1u8y" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1u8y, resolution 1.55&Aring;" />
caption="1u8y, resolution 1.55&Aring;" />
'''CRystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap'''<br />
'''CRystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap'''<br />


==Overview==
==Overview==
RalA is a GTPase with effectors such as Sec5 and Exo84 in the exocyst, complex and RalBP1, a GAP for Rho proteins. We report the crystal, structures of Ral-GppNHp and Ral-GDP. Disordered switch I and switch II, located away from crystal contacts, are observed in one of the molecules, in the asymmetric unit of the Ral-GppNHp structure. In the other molecule, in the asymmetric unit, a second Mg(2+) ion is bound to the GppNHp, gamma-phosphate in an environment in which switch I is pulled away from, the nucleotide and switch II is found in a tight beta turn. Clustering of, conserved residues on the surface of Ral-GppNHp identifies two putative, sites for protein-protein interaction. One site is adjacent to switch I., The other is modulated by switch II and is obstructed in Ral-GDP. The Ral, structures are discussed in the context of the published structures of the, Ral/Sec5 complex, Ras, and Rap.
RalA is a GTPase with effectors such as Sec5 and Exo84 in the exocyst complex and RalBP1, a GAP for Rho proteins. We report the crystal structures of Ral-GppNHp and Ral-GDP. Disordered switch I and switch II, located away from crystal contacts, are observed in one of the molecules in the asymmetric unit of the Ral-GppNHp structure. In the other molecule in the asymmetric unit, a second Mg(2+) ion is bound to the GppNHp gamma-phosphate in an environment in which switch I is pulled away from the nucleotide and switch II is found in a tight beta turn. Clustering of conserved residues on the surface of Ral-GppNHp identifies two putative sites for protein-protein interaction. One site is adjacent to switch I. The other is modulated by switch II and is obstructed in Ral-GDP. The Ral structures are discussed in the context of the published structures of the Ral/Sec5 complex, Ras, and Rap.


==About this Structure==
==About this Structure==
1U8Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saguinus_oedipus Saguinus oedipus] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U8Y OCA].  
1U8Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saguinus_oedipus Saguinus oedipus] 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=1U8Y OCA].  


==Reference==
==Reference==
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[[Category: Kosak, J.]]
[[Category: Kosak, J.]]
[[Category: Mattos, C.]]
[[Category: Mattos, C.]]
[[Category: Nicely, N.I.]]
[[Category: Nicely, N I.]]
[[Category: Serrano, V.de.]]
[[Category: Serrano, V de.]]
[[Category: GNP]]
[[Category: GNP]]
[[Category: MG]]
[[Category: MG]]
[[Category: signaling protein]]
[[Category: signaling protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:55:53 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:49 2008''

Revision as of 13:21, 21 February 2008

File:1u8y.jpg


1u8y, resolution 1.55Å

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CRystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap

Overview

RalA is a GTPase with effectors such as Sec5 and Exo84 in the exocyst complex and RalBP1, a GAP for Rho proteins. We report the crystal structures of Ral-GppNHp and Ral-GDP. Disordered switch I and switch II, located away from crystal contacts, are observed in one of the molecules in the asymmetric unit of the Ral-GppNHp structure. In the other molecule in the asymmetric unit, a second Mg(2+) ion is bound to the GppNHp gamma-phosphate in an environment in which switch I is pulled away from the nucleotide and switch II is found in a tight beta turn. Clustering of conserved residues on the surface of Ral-GppNHp identifies two putative sites for protein-protein interaction. One site is adjacent to switch I. The other is modulated by switch II and is obstructed in Ral-GDP. The Ral structures are discussed in the context of the published structures of the Ral/Sec5 complex, Ras, and Rap.

About this Structure

1U8Y is a Single protein structure of sequence from Saguinus oedipus with MG and GNP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap., Nicely NI, Kosak J, de Serrano V, Mattos C, Structure. 2004 Nov;12(11):2025-36. PMID:15530367

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