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1u90

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(New page: 200px<br /><applet load="1u90" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u90, resolution 2.00&Aring;" /> '''Crystal structures o...)
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[[Image:1u90.jpg|left|200px]]<br /><applet load="1u90" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u90.jpg|left|200px]]<br /><applet load="1u90" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u90, resolution 2.00&Aring;" />
caption="1u90, resolution 2.00&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==
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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.
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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==
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1U90 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 GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U90 OCA].
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1U90 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=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=1U90 OCA].
==Reference==
==Reference==
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[[Category: Kosak, J.]]
[[Category: Kosak, J.]]
[[Category: Mattos, C.]]
[[Category: Mattos, C.]]
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[[Category: Nicely, N.I.]]
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[[Category: Nicely, N I.]]
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[[Category: Serrano, V.de.]]
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[[Category: Serrano, V de.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: ras]]
[[Category: ras]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:56:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:52 2008''

Revision as of 13:21, 21 February 2008


1u90, resolution 2.00Å

Drag the structure with the mouse to rotate

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

1U90 is a Single protein structure of sequence from Saguinus oedipus with and 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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