1tu3

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(New page: 200px<br /> <applet load="1tu3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tu3, resolution 2.31&Aring;" /> '''Crystal Structure o...)
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[[Image:1tu3.gif|left|200px]]<br />
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[[Image:1tu3.gif|left|200px]]<br /><applet load="1tu3" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1tu3" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1tu3, resolution 2.31&Aring;" />
caption="1tu3, resolution 2.31&Aring;" />
'''Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain'''<br />
'''Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain'''<br />
==Overview==
==Overview==
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Rab5 is a small GTPase that regulates early endosome fusion. We present, here the crystal structure of the Rab5 GTPase domain in complex with a GTP, analog and the C-terminal domain of effector Rabaptin5. The proteins form, a dyad-symmetric Rab5-Rabaptin5(2)-Rab5 ternary complex with a parallel, coiled-coil Rabaptin5 homodimer in the middle. Two Rab5 molecules bind, independently to the Rabaptin5 dimer using their switch and interswitch, regions. The binding does not involve the Rab complementarity-determining, regions. We also present the crystal structures of two distinct forms of, GDP-Rab5 complexes, both of which are incompatible with Rabaptin5 binding., One has a dislocated and disordered switch I but a virtually intact switch, II, whereas the other has its beta-sheet and both switch regions, reorganized. Biochemical and functional analyses show that the, crystallographically observed Rab5-Rabaptin5 complex also exists in, solution, and disruption of this complex by mutation abrogates endosome, fusion.
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Rab5 is a small GTPase that regulates early endosome fusion. We present here the crystal structure of the Rab5 GTPase domain in complex with a GTP analog and the C-terminal domain of effector Rabaptin5. The proteins form a dyad-symmetric Rab5-Rabaptin5(2)-Rab5 ternary complex with a parallel coiled-coil Rabaptin5 homodimer in the middle. Two Rab5 molecules bind independently to the Rabaptin5 dimer using their switch and interswitch regions. The binding does not involve the Rab complementarity-determining regions. We also present the crystal structures of two distinct forms of GDP-Rab5 complexes, both of which are incompatible with Rabaptin5 binding. One has a dislocated and disordered switch I but a virtually intact switch II, whereas the other has its beta-sheet and both switch regions reorganized. Biochemical and functional analyses show that the crystallographically observed Rab5-Rabaptin5 complex also exists in solution, and disruption of this complex by mutation abrogates endosome fusion.
==About this Structure==
==About this Structure==
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1TU3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1TU3 OCA].
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1TU3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1TU3 OCA].
==Reference==
==Reference==
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[[Category: Terzyan, S.]]
[[Category: Terzyan, S.]]
[[Category: Zhai, P.]]
[[Category: Zhai, P.]]
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[[Category: Zhang, X.C.]]
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[[Category: Zhang, X C.]]
[[Category: Zhu, G.]]
[[Category: Zhu, G.]]
[[Category: GNP]]
[[Category: GNP]]
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[[Category: rabaptin5]]
[[Category: rabaptin5]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:28:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:23 2008''

Revision as of 13:17, 21 February 2008

Image:1tu3.gif

1tu3, resolution 2.31Å

Drag the structure with the mouse to rotate

Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain

Overview

Rab5 is a small GTPase that regulates early endosome fusion. We present here the crystal structure of the Rab5 GTPase domain in complex with a GTP analog and the C-terminal domain of effector Rabaptin5. The proteins form a dyad-symmetric Rab5-Rabaptin5(2)-Rab5 ternary complex with a parallel coiled-coil Rabaptin5 homodimer in the middle. Two Rab5 molecules bind independently to the Rabaptin5 dimer using their switch and interswitch regions. The binding does not involve the Rab complementarity-determining regions. We also present the crystal structures of two distinct forms of GDP-Rab5 complexes, both of which are incompatible with Rabaptin5 binding. One has a dislocated and disordered switch I but a virtually intact switch II, whereas the other has its beta-sheet and both switch regions reorganized. Biochemical and functional analyses show that the crystallographically observed Rab5-Rabaptin5 complex also exists in solution, and disruption of this complex by mutation abrogates endosome fusion.

About this Structure

1TU3 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis of Rab5-Rabaptin5 interaction in endocytosis., Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC, Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. PMID:15378032

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