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[[Image:2ffq.gif|left|200px]]


{{Structure
==The crystal structure of human neuronal Rab6B in its active GTPgS-bound form==
|PDB= 2ffq |SIZE=350|CAPTION= <scene name='initialview01'>2ffq</scene>, resolution 1.78&Aring;
<StructureSection load='2ffq' size='340' side='right'caption='[[2ffq]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>
<table><tr><td colspan='2'>[[2ffq]] is a 1 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=2FFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FFQ FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
|GENE= RAB6B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2ffq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ffq OCA], [https://pdbe.org/2ffq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ffq RCSB], [https://www.ebi.ac.uk/pdbsum/2ffq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ffq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RAB6B_HUMAN RAB6B_HUMAN] Seems to have a role in retrograde membrane traffic at the level of the Golgi complex. May function in retrograde transport in neuronal cells.<ref>PMID:17707369</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/ff/2ffq_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=2ffq ConSurf].
<div style="clear:both"></div>


'''The crystal structure of human neuronal Rab6B in its active GTPgS-bound form'''
==See Also==
 
*[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]]
 
== References ==
==Overview==
<references/>
The Rab small G-protein family plays important roles in eukaryotes as regulators of vesicle traffic. In Rab proteins, the hydrolysis of GTP to GDP is coupled with association with and dissociation from membranes. Conformational changes related to their different nucleotide states determine their effector specificity. The crystal structure of human neuronal Rab6B was solved in its 'inactive' (with bound MgGDP) and 'active' (MgGTPgammaS-bound) forms to 2.3 and 1.8 A, respectively. Both crystallized in space group P2(1)2(1)2(1), with similar unit-cell parameters, allowing the comparison of both structures without packing artifacts. Conformational changes between the inactive GDP and active GTP-like state are observed mainly in the switch I and switch II regions, confirming their role as a molecular switch. Compared with other Rab proteins, additional changes are observed in the Rab6 subfamily-specific RabSF3 region that might contribute to the specificity of Rab6 for its different effector proteins.
__TOC__
 
</StructureSection>
==About this Structure==
2FFQ is a [[Single protein]] structure of sequence 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=2FFQ OCA].
 
==Reference==
The structure of human neuronal Rab6B in the active and inactive form., Garcia-Saez I, Tcherniuk S, Kozielski F, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):725-33. Epub 2006, Jun 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16790928 16790928]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Garcia-Saez, I.]]
[[Category: Garcia-Saez I]]
[[Category: Kozielski, F.]]
[[Category: Kozielski F]]
[[Category: Tcherniuk, S.]]
[[Category: Tcherniuk S]]
[[Category: GSP]]
[[Category: MG]]
[[Category: protein-nucleotide complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:51:54 2008''
Retrieved from "https://proteopedia.org/2ffq"