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==Solution structure of myirstoylated yeast ARF1 protein, GDP-bound== | |||
<StructureSection load='2k5u' size='340' side='right'caption='[[2k5u]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2k5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K5U FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARF1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2k5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k5u OCA], [https://pdbe.org/2k5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k5u RCSB], [https://www.ebi.ac.uk/pdbsum/2k5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k5u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/ARF1_YEAST ARF1_YEAST]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.<ref>PMID:15356266</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k5/2k5u_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2k5u ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ADP-ribosylation factors (ARFs) are small (21 kDa), monomeric GTPases that are important regulators of membrane traffic. When membrane bound, they recruit soluble adaptors to membranes and trigger the assembly of coating complexes involved in cargo selection and vesicular budding. N-myristoylation is a conserved feature of all ARF proteins that is required for its biological functions, although the mechanism(s) by which the myristate acts in ARF functions is not fully understood. Here we present the structure of a myristoylated ARF1 protein, determined by solution NMR methods, and an assessment of the influence of myristoylation on association of ARF1.GDP and ARF1.GTP with lipid bilayers. A model in which myristoylation contributes to both the regulation of guanine nucleotide exchange and stable membrane association is supported. | |||
Structure and membrane interaction of myristoylated ARF1.,Liu Y, Kahn RA, Prestegard JH Structure. 2009 Jan 14;17(1):79-87. PMID:19141284<ref>PMID:19141284</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2k5u" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: | [[Category: Atcc 18824]] | ||
[[Category: Liu, Y | [[Category: Large Structures]] | ||
[[Category: Prestegard, J | [[Category: Liu, Y]] | ||
[[Category: Prestegard, J]] | |||
[[Category: Arf]] | [[Category: Arf]] | ||
[[Category: Arf1]] | [[Category: Arf1]] | ||
Latest revision as of 11:10, 7 April 2021
Solution structure of myirstoylated yeast ARF1 protein, GDP-boundSolution structure of myirstoylated yeast ARF1 protein, GDP-bound
Structural highlights
Function[ARF1_YEAST] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.[1] 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 PubMedADP-ribosylation factors (ARFs) are small (21 kDa), monomeric GTPases that are important regulators of membrane traffic. When membrane bound, they recruit soluble adaptors to membranes and trigger the assembly of coating complexes involved in cargo selection and vesicular budding. N-myristoylation is a conserved feature of all ARF proteins that is required for its biological functions, although the mechanism(s) by which the myristate acts in ARF functions is not fully understood. Here we present the structure of a myristoylated ARF1 protein, determined by solution NMR methods, and an assessment of the influence of myristoylation on association of ARF1.GDP and ARF1.GTP with lipid bilayers. A model in which myristoylation contributes to both the regulation of guanine nucleotide exchange and stable membrane association is supported. Structure and membrane interaction of myristoylated ARF1.,Liu Y, Kahn RA, Prestegard JH Structure. 2009 Jan 14;17(1):79-87. PMID:19141284[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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