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New page: left|200px<br /> <applet load="1hur" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hur, resolution 2.0Å" /> '''HUMAN ADP-RIBOSYLATI...
 
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[[Image:1hur.gif|left|200px]]<br />
<applet load="1hur" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hur, resolution 2.0&Aring;" />
'''HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED'''<br />


==Overview==
==HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED==
ADP-ribosylation factors (ARFs) are essential and ubiquitous in, eukaryotes, being involved in vesicular transport and functioning as an, activator of phospholipase D (refs 1, 2) and cholera toxin. The functions, of ARF proteins in membrane traffic and organelle integrity are intimately, tied to its reversible association with membranes and specific, interactions with membrane phospholipids. One common feature of these, functions is their regulation by the binding and hydrolysis of GTP. Here, we report the three-dimensional structure of full-length human ARF1 (M(r), 21,000) in its GDP-bound non-myristoylated form. The presence of a unique, amino-terminal alpha-helix and loop, together with differences in Mg2+, ligation and the existence of a non-crystallographic dimer, set this, structure apart from other GTP-binding proteins. These features provide a, structural basis for the GTP-dependent modulation of membrane affinity, the lack of intrinsic GTPase activity, and the nature of effector binding, surfaces.
<StructureSection load='1hur' size='340' side='right'caption='[[1hur]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1hur]] is a 2 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=1HUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HUR FirstGlance]. <br>
1HUR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HUR OCA].  
</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&#8491;</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hur OCA], [https://pdbe.org/1hur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hur RCSB], [https://www.ebi.ac.uk/pdbsum/1hur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hur ProSAT]</span></td></tr>
Structure of the human ADP-ribosylation factor 1 complexed with GDP., Amor JC, Harrison DH, Kahn RA, Ringe D, Nature. 1994 Dec 15;372(6507):704-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7990966 7990966]
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARF1_HUMAN ARF1_HUMAN] 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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/1hur_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=1hur ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Amor, J.C.]]
[[Category: Amor JC]]
[[Category: Harrison, D.H.]]
[[Category: Harrison DH]]
[[Category: Kahn, R.A.]]
[[Category: Kahn RA]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: GDP]]
[[Category: MG]]
[[Category: gdp-binding]]
[[Category: membrane traffickin]]
[[Category: non-myristoylated]]
 
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Latest revision as of 07:30, 7 February 2024

HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED

1hur, resolution 2.00Å

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