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2j59

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Crystal structure of the ARF1:ARHGAP21-ArfBD complex

Structural highlights

2j59 is a 12 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARF1_MOUSE GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Menetrey J, Perderiset M, Cicolari J, Dubois T, Elkhatib N, El Khadali F, Franco M, Chavrier P, Houdusse A. Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes. EMBO J. 2007 Apr 4;26(7):1953-62. Epub 2007 Mar 8. PMID:17347647

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j59"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the ARF1:ARHGAP21-ArfBD complex==
-<StructureSection load='2j59' size='340' side='right' caption='[[2j59]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='2j59' size='340' side='right'caption='[[2j59]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2j59]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J59 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2j59]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J59 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1o3y|1o3y]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j59 OCA], [http://pdbe.org/2j59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j59 RCSB], [http://www.ebi.ac.uk/pdbsum/2j59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j59 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j59 OCA], [https://pdbe.org/2j59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j59 RCSB], [https://www.ebi.ac.uk/pdbsum/2j59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j59 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RHG21_HUMAN RHG21_HUMAN]] Functions as a GTPase-activating protein (GAP) for RHOA and CDC42. Downstream partner of ARF1 which may control Golgi apparatus structure and function. Also required for CTNNA1 recruitment to adherens junctions.<ref>PMID:15793564</ref> <ref>PMID:16184169</ref>
+[https://www.uniprot.org/uniprot/ARF1_MOUSE ARF1_MOUSE] GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Rho GTPase activating protein|Rho GTPase activating protein]]
+*[[Rho GTPase activating protein 3D structures|Rho GTPase activating protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Chavrier, P]]
+[[Category: Mus musculus]]
-[[Category: Cicolari, J]]
+[[Category: Chavrier P]]
-[[Category: Dubois, T]]
+[[Category: Cicolari J]]
-[[Category: Franco, M]]
+[[Category: Dubois T]]
-[[Category: Houdusse, A]]
+[[Category: El Khadali F]]
-[[Category: Khadali, F El]]
+[[Category: El Khatib N]]
-[[Category: Khatib, N El]]
+[[Category: Franco M]]
-[[Category: Menetrey, J]]
+[[Category: Houdusse A]]
-[[Category: Perderiset, M]]
+[[Category: Menetrey J]]
-[[Category: Actin organization]]
+[[Category: Perderiset M]]
-[[Category: Arf]]
-[[Category: Arf1]]
-[[Category: Arfbd]]
-[[Category: Arhgap21]]
-[[Category: Golgi apparatus]]
-[[Category: Hydrolase]]
-[[Category: Myristate]]
-[[Category: Nucleotide-binding]]
-[[Category: Protein transport]]
-[[Category: Rhogap protein]]
-[[Category: Small gtp-binding protein]]
-[[Category: Transport]]

2j59

From Proteopedia

Current revision

Crystal structure of the ARF1:ARHGAP21-ArfBD complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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