1x79: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
New page: left|200px<br /> <applet load="1x79" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x79, resolution 2.41Å" /> '''Crystal structure o...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1x79.gif|left|200px]]<br />
<applet load="1x79" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1x79, resolution 2.41&Aring;" />
'''Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5'''<br />


==Overview==
==Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5==
GGA proteins coordinate the intracellular trafficking of clathrin-coated, vesicles through their interaction with several other proteins. The GAT, domain of GGA proteins interacts with ARF, ubiquitin, and Rabaptin5. The, GGA-Rabaptin5 interaction is believed to function in the fusion of, trans-Golgi-derived vesicles to endosomes. We determined the crystal, structure of a human GGA1 GAT domain fragment in complex with the, Rabaptin5 GAT-binding domain. In this structure, the Rabaptin5 domain is a, 90-residue-long helix. At the N-terminal end, it forms a parallel, coiled-coil homodimer, which binds one GAT domain of GGA1. In the, C-terminal region, it further assembles into a four-helix bundle tetramer., The Rabaptin5-binding motif of the GGA1 GAT domain consists of a, three-helix bundle. Thus, the binding between Rabaptin5 and GGA1 GAT, domain is based on a helix bundle-helix bundle interaction. The current, structural observation is consistent with previously reported mutagenesis, data, and its biological relevance is further confirmed by new mutagenesis, studies and affinity analysis. The four-helix bundle structure of, Rabaptin5 suggests a functional role in tethering organelles.
<StructureSection load='1x79' size='340' side='right'caption='[[1x79]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1x79]] is a 3 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=1X79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X79 FirstGlance]. <br>
1X79 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and DTT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X79 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]] 2.41&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1x79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x79 OCA], [https://pdbe.org/1x79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x79 RCSB], [https://www.ebi.ac.uk/pdbsum/1x79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x79 ProSAT]</span></td></tr>
Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5., Zhu G, Zhai P, He X, Wakeham N, Rodgers K, Li G, Tang J, Zhang XC, EMBO J. 2004 Oct 13;23(20):3909-17. Epub 2004 Sep 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15457209 15457209]
</table>
== Function ==
[https://www.uniprot.org/uniprot/GGA1_HUMAN GGA1_HUMAN] Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.<ref>PMID:11301005</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/x7/1x79_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=1x79 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Zhang, X.C.]]
[[Category: Zhang XC]]
[[Category: Zhu, G.]]
[[Category: Zhu G]]
[[Category: DTT]]
[[Category: SO4]]
[[Category: gat domain]]
[[Category: gga protein]]
[[Category: intracellular trafficking]]
[[Category: rabaptin5]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:01:36 2007''

Latest revision as of 08:48, 14 February 2024

Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5

1x79, resolution 2.41Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1x79&oldid=4056130"