Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt 7):692-4. doi: 10.1107/S1744309106023074. Epub 2006 Jun 26.

Abstract

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(1)21, with unit-cell parameters a = 64.99, b = 64.99, c = 112.59 angstroms. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Crystallization
  • Light
  • Protein Conformation
  • Scattering, Radiation
  • X-Ray Diffraction
  • rab GTP-Binding Proteins / chemistry*
  • rab GTP-Binding Proteins / isolation & purification
  • rab GTP-Binding Proteins / metabolism*

Substances

  • Carrier Proteins
  • rab11 protein
  • rab GTP-Binding Proteins