3BBP

Rab6-GTP:GCC185 Rab binding domain complex

Summary for 3BBP

• Entry DOI: 10.2210/pdb3bbp/pdb
• Related: 2GIL
• Descriptor: Ras-related protein Rab-6A, GRIP and coiled-coil domain-containing protein 2, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: golgi complex; grip domain; rab gtpase; arl gtpase; golgin; rab effector; clasp protein, acetylation, alternative splicing, er-golgi transport, golgi apparatus, gtp-binding, lipoprotein, membrane, methylation, nucleotide-binding, phosphorylation, prenylation, protein transport, transport, coiled coil, cytoplasm, polymorphism, protein transport-splicing complex, protein transport/splicing
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus membrane; Lipid-anchor: P20340; Cytoplasm: Q8IWJ2
• Total number of polymer chains: 6
• Total formula weight: 97661.58

Authors

Schweizer Burguete, A.,Fenn, T.D.,Brunger, A.T.,Pfeffer, S.R. (deposition date: 2007-11-09, release date: 2008-02-05, Last modification date: 2023-08-30)

Primary citation

Burguete, A.S.,Fenn, T.D.,Brunger, A.T.,Pfeffer, S.R.
Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185.
Cell(Cambridge,Mass.), 132:286-298, 2008

PubMed Abstract: GCC185 is a large coiled-coil protein at the trans Golgi network that is required for receipt of transport vesicles inbound from late endosomes and for anchoring noncentrosomal microtubules that emanate from the Golgi. Here, we demonstrate that recruitment of GCC185 to the Golgi is mediated by two Golgi-localized small GTPases of the Rab and Arl families. GCC185 binds Rab6, and mutation of residues needed for Rab binding abolishes Golgi localization. The crystal structure of Rab6 bound to the GCC185 Rab-binding domain reveals that Rab6 recognizes a two-fold symmetric surface on a coiled coil immediately adjacent to a C-terminal GRIP domain. Unexpectedly, Rab6 binding promotes association of Arl1 with the GRIP domain. We present a structure-derived model for dual GTPase membrane attachment that highlights the potential ability of Rab GTPases to reach binding partners at a significant distance from the membrane via their unstructured and membrane-anchored, hypervariable domains.

PubMed: 18243103
DOI: 10.1016/j.cell.2007.11.048

Experimental method

X-RAY DIFFRACTION (3 Å)