1rrg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1rrg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rrg, resolution 2.4Å" /> '''NON-MYRISTOYLATED RAT...
 
OCA (talk | contribs)
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1rrg.jpg|left|200px]]<br /><applet load="1rrg" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rrg, resolution 2.4&Aring;" />
'''NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM'''<br />


==Overview==
==NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM==
The ARFs are a family of 21,000 M(r) proteins with biological roles in, constitutive secretion and activation of phospholipase D. The structure of, ARF-1 complexed to GDP determined from two crystal forms reveals a, topology that is similar to that of the protein p21 ras with two, differences: an additional amino-terminal helix and an extra beta-strand., The Mg2+ ion in ARF-1 displays a five-coordination sphere; this feature is, not seen in p21 ras, due to a shift in the relative position of the DXXG, motif between the two proteins. The occurrence of a dimer in one crystal, form suggests that ARF-1 may dimerize during its biological function. The, dimer interface involves a region of the ARF-1 molecule that is analogous, to the effector domain in p21 ras and may mediate interactions with its, effectors.
<StructureSection load='1rrg' size='340' side='right'caption='[[1rrg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1rrg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RRG FirstGlance]. <br>
1RRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1RRG 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]] 2.4&#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=1rrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rrg OCA], [https://pdbe.org/1rrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rrg RCSB], [https://www.ebi.ac.uk/pdbsum/1rrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rrg ProSAT]</span></td></tr>
The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms., Greasley SE, Jhoti H, Teahan C, Solari R, Fensome A, Thomas GM, Cockcroft S, Bax B, Nat Struct Biol. 1995 Sep;2(9):797-806. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7552752 7552752]
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARF1_RAT ARF1_RAT] 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/rr/1rrg_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=1rrg ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Bax B]]
[[Category: Bax, B.]]
[[Category: Greasley SE]]
[[Category: Greasley, S.E.]]
[[Category: Jhoti H]]
[[Category: Jhoti, H.]]
[[Category: GDP]]
[[Category: MG]]
[[Category: gdp-binding]]
[[Category: homodimer]]
[[Category: membrane trafficking]]
[[Category: transport protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:49:17 2007''

Latest revision as of 08:25, 14 February 2024

NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM

1rrg, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA