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| <StructureSection load='1r4a' size='340' side='right'caption='[[1r4a]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1r4a' size='340' side='right'caption='[[1r4a]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1r4a]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R4A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r4a]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4A FirstGlance]. <br> |
- | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=10116 Buffalo rat]), GOLGIN-245 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4a OCA], [http://pdbe.org/1r4a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r4a RCSB], [http://www.ebi.ac.uk/pdbsum/1r4a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4a 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=1r4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4a OCA], [https://pdbe.org/1r4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4a RCSB], [https://www.ebi.ac.uk/pdbsum/1r4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4a ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/ARL1_RAT ARL1_RAT]] GTP-binding protein. Can activate phospholipase D with very low efficiency (By similarity). Important for normal function of the Golgi apparatus.<ref>PMID:11792819</ref> <ref>PMID:12972563</ref> [[http://www.uniprot.org/uniprot/GOGA4_HUMAN GOGA4_HUMAN]] May play a role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with MACF1.<ref>PMID:15265687</ref> | + | [https://www.uniprot.org/uniprot/ARL1_RAT ARL1_RAT] GTP-binding protein. Can activate phospholipase D with very low efficiency (By similarity). Important for normal function of the Golgi apparatus.<ref>PMID:11792819</ref> <ref>PMID:12972563</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Buffalo rat]] | + | [[Category: Homo sapiens]] |
- | [[Category: Human]]
| + | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Hong, W]] | + | [[Category: Rattus norvegicus]] |
- | [[Category: Lu, L]] | + | [[Category: Hong W]] |
- | [[Category: Song, H]] | + | [[Category: Lu L]] |
- | [[Category: Wu, M]] | + | [[Category: Song H]] |
- | [[Category: Protein transport]]
| + | [[Category: Wu M]] |
- | [[Category: Ras-like g protein structure]]
| + | |
- | [[Category: Three-helix grip domain]]
| + | |
| Structural highlights
Function
ARL1_RAT GTP-binding protein. Can activate phospholipase D with very low efficiency (By similarity). Important for normal function of the Golgi apparatus.[1] [2]
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
Recruitment of the GRIP domain golgins to the trans-Golgi network is mediated by Arl1, a member of the ARF/Arl small GTPase family, through interaction between their GRIP domains and Arl1-GTP. The crystal structure of Arl1-GTP in complex with the GRIP domain of golgin-245 shows that Arl1-GTP interacts with the GRIP domain predominantly in a hydrophobic manner, with the switch II region conferring the main recognition surface. The involvement of the switch and interswitch regions in the interaction between Arl1-GTP and GRIP accounts for the specificity of GRIP domain for Arl1-GTP. Mutations that abolished the Arl1-mediated Golgi localization of GRIP domain golgins have been mapped on the interface between Arl1-GTP and GRIP. Notably, the GRIP domain forms a homodimer in which each subunit interacts separately with one Arl1-GTP. Mutations disrupting the GRIP domain dimerization also abrogated its Golgi targeting, suggesting that the dimeric form of GRIP domain is a functional unit.
Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1.,Wu M, Lu L, Hong W, Song H Nat Struct Mol Biol. 2004 Jan;11(1):86-94. Epub 2003 Dec 29. PMID:14718928[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu L, Horstmann H, Ng C, Hong W. Regulation of Golgi structure and function by ARF-like protein 1 (Arl1). J Cell Sci. 2001 Dec;114(Pt 24):4543-55. PMID:11792819
- ↑ Lu L, Hong W. Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi. Mol Biol Cell. 2003 Sep;14(9):3767-81. Epub 2003 May 18. PMID:12972563 doi:http://dx.doi.org/10.1091/mbc.E03-01-0864
- ↑ Wu M, Lu L, Hong W, Song H. Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1. Nat Struct Mol Biol. 2004 Jan;11(1):86-94. Epub 2003 Dec 29. PMID:14718928 doi:10.1038/nsmb714
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