2hv8

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(New page: 200px<br /> <applet load="2hv8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hv8, resolution 1.86&Aring;" /> '''Crystal structure o...)
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<applet load="2hv8" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2hv8, resolution 1.86&Aring;" />
caption="2hv8, resolution 1.86&Aring;" />
'''Crystal structure of GTP-bound Rab11 in complex with FIP3'''<br />
'''Crystal structure of GTP-bound Rab11 in complex with FIP3'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HV8 OCA].
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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.]]
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[[Category: Lambright, D.G.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:36:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:04 2008''

Revision as of 15:46, 21 February 2008


2hv8, resolution 1.86Å

Drag the structure with the mouse to rotate

Crystal structure of GTP-bound Rab11 in complex with FIP3

Overview

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

2HV8 is a Protein complex structure of sequences from Homo sapiens with , , , and as ligands. Full crystallographic information is available from OCA.

Reference

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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