3CWZ

Structure of RAB6(GTP)-R6IP1 complex

Summary for 3CWZ

• Entry DOI: 10.2210/pdb3cwz/pdb
• Related: 1D5C 1LOX 2DWK 2GIL 3BBP
• Descriptor: Ras-related protein Rab-6A, Rab6-interacting protein 1, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: rab6 interacting protein 1, rab small gtpase, rab-binding domain, guanosine 5' triphosphate, run, rpip8, unc-14, nesca plat, golgi apparatus, golgi, lipase, lipoxygenase, membrane, lipoprotein, er-golgi transport, gtp-binding, methylation, nucleotide-binding, phosphoprotein, prenylation, protein transport, transport, transport protein
• Biological source: Homo sapiens (man); More
• Cellular location: Golgi apparatus membrane ; Lipid-anchor . Isoform 1: Golgi apparatus membrane ; Lipid-anchor . Isoform 2: Golgi apparatus membrane ; Lipid-anchor : P20340; Golgi apparatus membrane : Q6PAL8
• Total number of polymer chains: 2
• Total formula weight: 66164.96

Authors

Recacha, R.,Houdusse, A.,Goud, B.,Khan, A.R. (deposition date: 2008-04-23, release date: 2008-11-18, Last modification date: 2024-02-21)

Primary citation

Recacha, R.,Boulet, A.,Jollivet, F.,Monier, S.,Houdusse, A.,Goud, B.,Khan, A.R.
Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain.
Structure, 17:21-30, 2009

PubMed Abstract: Small GTPase Rab6 regulates vesicle trafficking at the level of Golgi via recruitment of numerous and unrelated effectors. The crystal structure of Rab6a(GTP) in complex with a 378-residue internal fragment of the effector Rab6IP1 was solved at 3.2 angstroms resolution. This Rab6IP1 region encompasses an all alpha-helical RUN domain followed in tandem by a PLAT domain that adopts a beta sandwich fold. The structure reveals that the first and last alpha helices of the RUN domain mediate binding to switch I, switch II, and the interswitch region of Rab6. It represents the largest Rab-effector complex determined to date. Comparisons with the recent structure of Rab6 in complex with an unrelated effector, human golgin GCC185, reveals significant conformational changes in the conserved hydrophobic triad of Rab6. Flexibility in the switch and interswitch regions of Rab6 mediates recognition of compositionally distinct alpha-helical coiled coils, thereby contributing to Rab6 promiscuity in effector recruitment.

PubMed: 19141279
DOI: 10.1016/j.str.2008.10.014

Experimental method

X-RAY DIFFRACTION (3.2 Å)