1upt

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[[Image:1upt.jpg|left|200px]]
 
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{{Structure
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==Structure of a complex of the golgin-245 GRIP domain with Arl1==
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|PDB= 1upt |SIZE=350|CAPTION= <scene name='initialview01'>1upt</scene>, resolution 1.70&Aring;
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<StructureSection load='1upt' size='340' side='right'caption='[[1upt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+G'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene>
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<table><tr><td colspan='2'>[[1upt]] is a 8 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=1UPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UPT FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1upt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1upt OCA], [https://pdbe.org/1upt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1upt RCSB], [https://www.ebi.ac.uk/pdbsum/1upt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1upt ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF A COMPLEX OF THE GOLGIN-245 GRIP DOMAIN WITH ARL1'''
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== Function ==
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[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>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/up/1upt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1upt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Golgins are large coiled-coil proteins that play a role in Golgi structure and vesicle traffic. The Arf-like GTPase Arl1 regulates the translocation of GRIP domain-containing golgins to Golgi membranes. We report here the 1.7 A resolution structure of human Arl1-GTP in a complex with the GRIP domain of golgin-245. The structure reveals that the GRIP domain consists of an S-shaped arrangement of three helices. The domain forms a homodimer that binds two Arl1-GTPs using two helices from each monomer. The structure is consistent with golgin-245 forming parallel coiled-coils and suggests how Arl1-GTP/GRIP complexes interact with Golgi membranes via the N termini of Arl1-GTP and the C-terminal tails of the GRIP domains. In cells, bivalent association with Arl1-GTP would increase residence time of the golgins on Golgi membranes. Despite no conservation of sequence, topology, or even helical direction, several other effectors form similar interactions with small GTPases via a pair of alpha helices, suggesting a common structural basis for effector recognition.
Golgins are large coiled-coil proteins that play a role in Golgi structure and vesicle traffic. The Arf-like GTPase Arl1 regulates the translocation of GRIP domain-containing golgins to Golgi membranes. We report here the 1.7 A resolution structure of human Arl1-GTP in a complex with the GRIP domain of golgin-245. The structure reveals that the GRIP domain consists of an S-shaped arrangement of three helices. The domain forms a homodimer that binds two Arl1-GTPs using two helices from each monomer. The structure is consistent with golgin-245 forming parallel coiled-coils and suggests how Arl1-GTP/GRIP complexes interact with Golgi membranes via the N termini of Arl1-GTP and the C-terminal tails of the GRIP domains. In cells, bivalent association with Arl1-GTP would increase residence time of the golgins on Golgi membranes. Despite no conservation of sequence, topology, or even helical direction, several other effectors form similar interactions with small GTPases via a pair of alpha helices, suggesting a common structural basis for effector recognition.
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==Disease==
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Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus.,Panic B, Perisic O, Veprintsev DB, Williams RL, Munro S Mol Cell. 2003 Oct;12(4):863-74. PMID:14580338<ref>PMID:14580338</ref>
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Known disease associated with this structure: Leukemia, chronic lymphatic, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609351 609351]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1UPT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPT OCA].
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</div>
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<div class="pdbe-citations 1upt" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus., Panic B, Perisic O, Veprintsev DB, Williams RL, Munro S, Mol Cell. 2003 Oct;12(4):863-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14580338 14580338]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Munro, S.]]
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[[Category: Munro S]]
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[[Category: Panic, B.]]
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[[Category: Panic B]]
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[[Category: Perisic, O.]]
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[[Category: Perisic O]]
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[[Category: Veprintsev, D B.]]
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[[Category: Veprintsev DB]]
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[[Category: Williams, R L.]]
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[[Category: Williams RL]]
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[[Category: GTP]]
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[[Category: MG]]
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[[Category: arl1]]
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[[Category: g-protein]]
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[[Category: golgi]]
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[[Category: golgin]]
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[[Category: golgin-245]]
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[[Category: grip]]
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[[Category: grip dimer]]
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[[Category: gtpase]]
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[[Category: protein sorting]]
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[[Category: vesicle trafficking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:17 2008''
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Current revision

Structure of a complex of the golgin-245 GRIP domain with Arl1

PDB ID 1upt

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