2hv8: Difference between revisions
New page: left|200px<br /> <applet load="2hv8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hv8, resolution 1.86Å" /> '''Crystal structure o... |
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[[Image:2hv8.gif|left|200px]]<br /> | [[Image:2hv8.gif|left|200px]]<br /><applet load="2hv8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2hv8, resolution 1.86Å" /> | caption="2hv8, resolution 1.86Å" /> | ||
'''Crystal structure of GTP-bound Rab11 in complex with FIP3'''<br /> | '''Crystal structure of GTP-bound Rab11 in complex with FIP3'''<br /> | ||
==Overview== | ==Overview== | ||
The Rab11 GTPase regulates recycling of internalized plasma membrane | The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognize the active form of Rab11. Normal completion of cytokinesis requires a complex between Rab11 and FIP3. Here, we report the crystal structure and mutational analysis of a heterotetrameric complex between constitutively active Rab11 and a FIP3 construct that includes the RBD. Two Rab11 molecules bind to dyad symmetric sites at the C terminus of FIP3, which forms a non-canonical coiled-coiled dimer with a flared C terminus and hook region. The RBD overlaps with the coiled coil and extends through the C-terminal hook. Although FIP3 engages the switch and interswitch regions of Rab11, the mode of interaction differs significantly from that of other Rab-effector complexes. In particular, the switch II region undergoes a large structural rearrangement from an ordered but non-complementary active conformation to a remodeled conformation that facilitates the interaction with FIP3. Finally, we provide evidence that FIP3 can form homo-oligomers in cells, and that a critical determinant of Rab11 binding in vitro is necessary for FIP3 recruitment to recycling endosomes during cytokinesis. | ||
==About this Structure== | ==About this Structure== | ||
2HV8 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 2ME, MG, SO4, GTP and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2HV8 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 <scene name='pdbligand=2ME:'>2ME</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=GTP:'>GTP</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HV8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Eathiraj, S.]] | [[Category: Eathiraj, S.]] | ||
[[Category: Lambright, D | [[Category: Lambright, D G.]] | ||
[[Category: Mishra, A.]] | [[Category: Mishra, A.]] | ||
[[Category: Prekeris, R.]] | [[Category: Prekeris, R.]] | ||
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[[Category: recycling endosomes]] | [[Category: recycling endosomes]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:04 2008'' | ||
Revision as of 18:46, 21 February 2008
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Crystal structure of GTP-bound Rab11 in complex with FIP3
OverviewOverview
The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognize the active form of Rab11. Normal completion of cytokinesis requires a complex between Rab11 and FIP3. Here, we report the crystal structure and mutational analysis of a heterotetrameric complex between constitutively active Rab11 and a FIP3 construct that includes the RBD. Two Rab11 molecules bind to dyad symmetric sites at the C terminus of FIP3, which forms a non-canonical coiled-coiled dimer with a flared C terminus and hook region. The RBD overlaps with the coiled coil and extends through the C-terminal hook. Although FIP3 engages the switch and interswitch regions of Rab11, the mode of interaction differs significantly from that of other Rab-effector complexes. In particular, the switch II region undergoes a large structural rearrangement from an ordered but non-complementary active conformation to a remodeled conformation that facilitates the interaction with FIP3. Finally, we provide evidence that FIP3 can form homo-oligomers in cells, and that a critical determinant of Rab11 binding in vitro is necessary for FIP3 recruitment to recycling endosomes during cytokinesis.
About this StructureAbout this Structure
2HV8 is a Protein complex structure of sequences from Homo sapiens with , , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes., Eathiraj S, Mishra A, Prekeris R, Lambright DG, J Mol Biol. 2006 Nov 24;364(2):121-35. Epub 2006 Aug 26. PMID:17007872
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