2K6S

Structure of Rab11-FIP2 C-terminal Coiled-coil Domain

Summary for 2K6S

• Entry DOI: 10.2210/pdb2k6s/pdb
• NMR Information: BMRB: 15880
• Descriptor: Rab11fip2 protein (1 entity in total)
• Functional Keywords: rab11-fip2, coiled-coil domain, solution structure, protein transport
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 10009.57

Authors

Wei, J.,Liu, Y.,Baleja, J.D. (deposition date: 2008-07-18, release date: 2009-06-16, Last modification date: 2024-05-08)

Primary citation

Wei, J.,Liu, Y.,Bose, K.,Henry, G.D.,Baleja, J.D.
Disorder and structure in the Rab11 binding domain of Rab11 family interacting protein 2.
Biochemistry, 48:549-557, 2009

PubMed Abstract: Rab11 plays a central role in plasma membrane recycling which returns cellular receptors for reuse at the cell surface. A recently identified family of Rab11 interacting proteins (FIP) includes FIP2. The C-terminal region of FIP2 is essential for colocalization with Rab11 on early endosomes and for enabling formation of higher-order oligomers. Rab11 binding and oligomerization of FIP2 are separable. Here we have determined the three-dimensional structure of the 40-residue coiled-coil oligomerization domain of FIP2 in the absence of Rab11 using NMR methods. The N-terminal half showed strong NOE cross-peaks and well-dispersed NMR resonances, whereas the C-terminal half had fewer NOE cross-peaks and less chemical shift dispersion. The 10 C-terminal residues were mostly disordered. The final structures of the dimer had favorable Ramachandran angles and a root-mean-square deviation of 0.59 +/- 0.13 A over superimposed backbone residues. The structure allows a comparison to a structure of FIP2 in complex with Rab11 that was determined crystallographically. In complex with Rab11, the C-terminal residues are not disordered but have a helical structure that predicts residual dipolar coupling constants that are incompatible with those measured on the unbound FIP2. In both structures, a histidine residue is found at the normally hydrophobic position of the heptad repeat of the coiled coil, and here we show its ionization destabilizes the coiled-coil structure. Together, these data allow us to build a model in which the binding of FIP family proteins to Rab11 can be described in terms of conformational changes and that suggests new modes of regulation.

PubMed: 19119858
DOI: 10.1021/bi8020197

Experimental method

SOLUTION NMR