Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2
- School of Biochemistry and Immunology, Trinity College, Dublin 2 (Ireland)
- Molecular Cell Biology Laboratory, Department of Biochemistry, Biosciences Institute, University College Cork, Cork (Ireland)
Crystals of Rab11 in complex with the Rab-binding domain (RBD) of its effector Rab11-FIP2 were grown and synchrotron diffraction data were collected at 2.8 Å resolution. The small GTPase Rab11 regulates the recycling of endosomes back to the plasma membrane. In its active GTP-bound form, Rab11 binds a novel set of effectors termed the Rab11 family of interacting proteins (Rab11-FIPs) which contain a conserved C-terminal Rab-binding domain (RBD) of unknown structure. Here, a complex of Rab11 with the RBD of Rab11-FIP2 has been purified and crystallized in the trigonal space group P3{sub 1}21, with unit-cell parameters a = 64.99, b = 64.99, c = 112.59 Å. Static light-scattering analyses of the molecular weight of the complex in solution are consistent with two copies of Rab11 and two copies of Rab11-FIP2 in the complex.
- OSTI ID:
- 22360191
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 7; Other Information: PMCID: PMC2242937; PMID: 16820696; PUBLISHER-ID: bo5001; OAI: oai:pubmedcentral.nih.gov:2242937; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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