2j59
From Proteopedia
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| - | [[Image:2j59.gif|left|200px]]<br /> | + | [[Image:2j59.gif|left|200px]]<br /><applet load="2j59" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2j59" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2j59, resolution 2.1Å" /> | caption="2j59, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ARF1:ARHGAP21-ARFBD COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF THE ARF1:ARHGAP21-ARFBD COMPLEX'''<br /> | ||
| + | |||
| + | ==Overview== | ||
| + | ARHGAP21 is a Rho family GTPase-activating protein (RhoGAP) that controls, the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating, the activity of the small GTPase Cdc42. ARHGAP21 is recruited to the Golgi, by binding to another small GTPase, ARF1. Here, we present the crystal, structure of the activated GTP-bound form of ARF1 in a complex with the, Arf-binding domain (ArfBD) of ARHGAP21 at 2.1 A resolution. We show that, ArfBD comprises a PH domain adjoining a C-terminal alpha helix, and that, ARF1 interacts with both of these structural motifs through its switch, regions and triggers structural rearrangement of the PH domain. We used, site-directed mutagenesis to confirm that both the PH domain and the, helical motif are essential for the binding of ArfBD to ARF1 and for its, recruitment to the Golgi. Our data demonstrate that two well-known small, GTPase-binding motifs, the PH domain and the alpha helical motif, can, combine to create a novel mode of binding to Arfs. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2J59 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG, SO4, GTP, DIO and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2J59 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG, SO4, GTP, DIO and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Gtp Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Mg Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Gtp Binding Site For Chain B'>AC3</scene>, <scene name='pdbsite=AC4:Mg Binding Site For Chain B'>AC4</scene>, <scene name='pdbsite=AC5:Gtp Binding Site For Chain C'>AC5</scene>, <scene name='pdbsite=AC6:Mg Binding Site For Chain C'>AC6</scene>, <scene name='pdbsite=AC7:Gtp Binding Site For Chain D'>AC7</scene>, <scene name='pdbsite=AC8:Mg Binding Site For Chain D'>AC8</scene>, <scene name='pdbsite=AC9:Gtp Binding Site For Chain E'>AC9</scene>, <scene name='pdbsite=BC1:Mg Binding Site For Chain E'>BC1</scene>, <scene name='pdbsite=BC2:Gtp Binding Site For Chain F'>BC2</scene>, <scene name='pdbsite=BC3:Mg Binding Site For Chain F'>BC3</scene>, <scene name='pdbsite=BC4:So4 Binding Site For Chain M'>BC4</scene>, <scene name='pdbsite=BC5:So4 Binding Site For Chain N'>BC5</scene>, <scene name='pdbsite=BC6:So4 Binding Site For Chain O'>BC6</scene>, <scene name='pdbsite=BC7:So4 Binding Site For Chain P'>BC7</scene>, <scene name='pdbsite=BC8:So4 Binding Site For Chain Q'>BC8</scene>, <scene name='pdbsite=BC9:So4 Binding Site For Chain R'>BC9</scene>, <scene name='pdbsite=CC1:Dio Binding Site For Chain A'>CC1</scene>, <scene name='pdbsite=CC2:Dio Binding Site For Chain B'>CC2</scene>, <scene name='pdbsite=CC3:Dio Binding Site For Chain F'>CC3</scene>, <scene name='pdbsite=CC4:Edo Binding Site For Chain C'>CC4</scene>, <scene name='pdbsite=CC5:Edo Binding Site For Chain O'>CC5</scene> and <scene name='pdbsite=CC6:Edo Binding Site For Chain E'>CC6</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J59 OCA]. |
| + | |||
| + | ==Reference== | ||
| + | Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes., Menetrey J, Perderiset M, Cicolari J, Dubois T, Elkhatib N, El Khadali F, Franco M, Chavrier P, Houdusse A, EMBO J. 2007 Apr 4;26(7):1953-62. Epub 2007 Mar 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17347647 17347647] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:49:27 2007'' |
Revision as of 17:39, 18 December 2007
|
CRYSTAL STRUCTURE OF THE ARF1:ARHGAP21-ARFBD COMPLEX
Overview
ARHGAP21 is a Rho family GTPase-activating protein (RhoGAP) that controls, the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating, the activity of the small GTPase Cdc42. ARHGAP21 is recruited to the Golgi, by binding to another small GTPase, ARF1. Here, we present the crystal, structure of the activated GTP-bound form of ARF1 in a complex with the, Arf-binding domain (ArfBD) of ARHGAP21 at 2.1 A resolution. We show that, ArfBD comprises a PH domain adjoining a C-terminal alpha helix, and that, ARF1 interacts with both of these structural motifs through its switch, regions and triggers structural rearrangement of the PH domain. We used, site-directed mutagenesis to confirm that both the PH domain and the, helical motif are essential for the binding of ArfBD to ARF1 and for its, recruitment to the Golgi. Our data demonstrate that two well-known small, GTPase-binding motifs, the PH domain and the alpha helical motif, can, combine to create a novel mode of binding to Arfs.
About this Structure
2J59 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with MG, SO4, GTP, DIO and EDO as ligands. Known structural/functional Sites: , , , , , , , , , , , , , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes., Menetrey J, Perderiset M, Cicolari J, Dubois T, Elkhatib N, El Khadali F, Franco M, Chavrier P, Houdusse A, EMBO J. 2007 Apr 4;26(7):1953-62. Epub 2007 Mar 8. PMID:17347647
Page seeded by OCA on Tue Dec 18 19:49:27 2007
Categories: Homo sapiens | Mus musculus | Protein complex | Chavrier, P. | Cicolari, J. | Dubois, T. | Franco, M. | Houdusse, A. | Khadali, F.El. | Khatib, N.El. | Menetrey, J. | Perderiset, M. | DIO | EDO | GTP | MG | SO4 | Actin organization | Arf | Arf1 | Arfbd | Arhgap21 | Golgi apparatus | Hydrolase | Myristate | Nucleotide-binding | Protein transport | Rhogap protein | Small gtp-binding protein | Transport
