4q9u: Difference between revisions
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''' | ==Crystal structure of the Rab5, Rabex-5delta and Rabaptin-5C21 complex== | ||
<StructureSection load='4q9u' size='340' side='right' caption='[[4q9u]], [[Resolution|resolution]] 4.62Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4q9u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q9U FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n3x|4n3x]], [[4n3y|4n3y]], [[4n3z|4n3z]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q9u RCSB], [http://www.ebi.ac.uk/pdbsum/4q9u PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rabex-5 and Rabaptin-5 function together to activate Rab5 and further promote early endosomal fusion in endocytosis. The Rabex-5 GEF activity is autoinhibited by the Rabex-5 CC domain (Rabex-5CC) and activated by the Rabaptin-5 C2-1 domain (Rabaptin-5C21) with yet unknown mechanism. We report here the crystal structures of Rabex-5 in complex with the dimeric Rabaptin-5C21 (Rabaptin-5C212) and in complex with Rabaptin-5C212 and Rab5, along with biophysical and biochemical analyses. We show that Rabex-5CC assumes an amphipathic alpha-helix which binds weakly to the substrate-binding site of the GEF domain, leading to weak autoinhibition of the GEF activity. Binding of Rabaptin-5C21 to Rabex-5 displaces Rabex-5CC to yield a largely exposed substrate-binding site, leading to release of the GEF activity. In the ternary complex the substrate-binding site of Rabex-5 is completely exposed to bind and activate Rab5. Our results reveal the molecular mechanism for the regulation of the Rabex-5 GEF activity. | |||
Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5.,Zhang Z, Zhang T, Wang S, Gong Z, Tang C, Chen J, Ding J Elife (Cambridge). 2014 Jun 23:e02687. doi: 10.7554/eLife.02687. PMID:24957337<ref>PMID:24957337</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ding, J.]] | |||
[[Category: Zhang, T.]] | |||
[[Category: Zhang, Z.]] | |||
[[Category: Coiled-coil]] | |||
[[Category: Early endosome]] | |||
[[Category: Effector]] | |||
[[Category: Endocytosis]] | |||
[[Category: Gef]] | |||
[[Category: Gef activity]] | |||
[[Category: Rab5]] | |||
[[Category: Rabaptin-5]] | |||
[[Category: Rabex-5]] | |||
[[Category: Small gtpase]] | |||
[[Category: Vps9]] | |||
Revision as of 10:56, 23 July 2014
Crystal structure of the Rab5, Rabex-5delta and Rabaptin-5C21 complexCrystal structure of the Rab5, Rabex-5delta and Rabaptin-5C21 complex
Structural highlights
Publication Abstract from PubMedRabex-5 and Rabaptin-5 function together to activate Rab5 and further promote early endosomal fusion in endocytosis. The Rabex-5 GEF activity is autoinhibited by the Rabex-5 CC domain (Rabex-5CC) and activated by the Rabaptin-5 C2-1 domain (Rabaptin-5C21) with yet unknown mechanism. We report here the crystal structures of Rabex-5 in complex with the dimeric Rabaptin-5C21 (Rabaptin-5C212) and in complex with Rabaptin-5C212 and Rab5, along with biophysical and biochemical analyses. We show that Rabex-5CC assumes an amphipathic alpha-helix which binds weakly to the substrate-binding site of the GEF domain, leading to weak autoinhibition of the GEF activity. Binding of Rabaptin-5C21 to Rabex-5 displaces Rabex-5CC to yield a largely exposed substrate-binding site, leading to release of the GEF activity. In the ternary complex the substrate-binding site of Rabex-5 is completely exposed to bind and activate Rab5. Our results reveal the molecular mechanism for the regulation of the Rabex-5 GEF activity. Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5.,Zhang Z, Zhang T, Wang S, Gong Z, Tang C, Chen J, Ding J Elife (Cambridge). 2014 Jun 23:e02687. doi: 10.7554/eLife.02687. PMID:24957337[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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