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| | ==Crystal Structure Analysis of the Arfaptin2 BAR domain in Complex with ARL1== | | ==Crystal Structure Analysis of the Arfaptin2 BAR domain in Complex with ARL1== |
| - | <StructureSection load='4dcn' size='340' side='right' caption='[[4dcn]], [[Resolution|resolution]] 3.01Å' scene=''> | + | <StructureSection load='4dcn' size='340' side='right'caption='[[4dcn]], [[Resolution|resolution]] 3.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dcn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DCN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DCN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dcn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DCN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1moz|1moz]], [[1upt|1upt]], [[1i49|1i49]], [[1i4l|1i4l]], [[3dyt|3dyt]]</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=4dcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dcn OCA], [https://pdbe.org/4dcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dcn RCSB], [https://www.ebi.ac.uk/pdbsum/4dcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dcn ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ARFIP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4dcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dcn OCA], [http://pdbe.org/4dcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dcn RCSB], [http://www.ebi.ac.uk/pdbsum/4dcn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dcn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ARL1_HUMAN ARL1_HUMAN]] GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus.<ref>PMID:9624189</ref> [[http://www.uniprot.org/uniprot/ARFP2_HUMAN ARFP2_HUMAN]] Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling. | + | [[https://www.uniprot.org/uniprot/ARL1_HUMAN ARL1_HUMAN]] GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus.<ref>PMID:9624189</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kato, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Kawasaki, M]] | + | [[Category: Kato R]] |
| - | [[Category: Nakamura, K]] | + | [[Category: Kawasaki M]] |
| - | [[Category: Wakatsuki, S]] | + | [[Category: Nakamura K]] |
| - | [[Category: Xie, Y]] | + | [[Category: Wakatsuki S]] |
| - | [[Category: Bar domain]]
| + | [[Category: Xie Y]] |
| - | [[Category: Membrane deformation]]
| + | |
| - | [[Category: Protein binding-signaling protein complex]]
| + | |
| - | [[Category: Small gtpase effector complex]]
| + | |
| Structural highlights
Function
[ARL1_HUMAN] GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus.[1]
Publication Abstract from PubMed
Membrane-sculpting BAR (Bin/Amphiphysin/Rvs) domains form a crescent-shaped homodimer that can sense and induce membrane curvature through its positively charged concave face. We have recently shown that Arfaptin-2, which was originally identified as a binding partner for the Arf and Rac1 GTPases, binds to Arl1 through its BAR domain and is recruited onto Golgi membranes. There, Arfaptin-2 induces membrane tubules. Here, we report the crystal structure of the Arfaptin-2 BAR homodimer in complex with two Arl1 molecules bound symmetrically to each side, leaving the concave face open for membrane association. The overall structure of the Arl1.Arfaptin-2 BAR complex closely resembles that of the PX-BAR domain of sorting nexin 9, suggesting similar mechanisms underlying BAR domain targeting to specific organellar membranes. The Arl1.Arfaptin-2 BAR structure suggests that one of the two Arl1 molecules competes with Rac1, which binds to the concave face of the Arfaptin-2 BAR homodimer and may hinder its membrane association.
Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase.,Nakamura K, Man Z, Xie Y, Hanai A, Makyio H, Kawasaki M, Kato R, Shin HW, Nakayama K, Wakatsuki S J Biol Chem. 2012 Jul 20;287(30):25478-89. doi: 10.1074/jbc.M112.365783. Epub, 2012 Jun 7. PMID:22679020[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hong JX, Lee FJ, Patton WA, Lin CY, Moss J, Vaughan M. Phospholipid- and GTP-dependent activation of cholera toxin and phospholipase D by human ADP-ribosylation factor-like protein 1 (HARL1). J Biol Chem. 1998 Jun 19;273(25):15872-6. PMID:9624189
- ↑ Nakamura K, Man Z, Xie Y, Hanai A, Makyio H, Kawasaki M, Kato R, Shin HW, Nakayama K, Wakatsuki S. Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase. J Biol Chem. 2012 Jul 20;287(30):25478-89. doi: 10.1074/jbc.M112.365783. Epub, 2012 Jun 7. PMID:22679020 doi:10.1074/jbc.M112.365783
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