1HK6

Ral binding domain from Sec5

Summary for 1HK6

• Entry DOI: 10.2210/pdb1hk6/pdb
• Descriptor: EXOCYST COMPLEX COMPONENT SEC5 (1 entity in total)
• Functional Keywords: ipt ral sec5 exocyst, exocytosis, protein transport, immunoglobulin fold
• Biological source: MUS MUSCULUS (MOUSE)
• Cellular location: Midbody, Midbody ring : Q9D4H1
• Total number of polymer chains: 1
• Total formula weight: 10114.77

Authors

Mott, H.R.,Nietlispach, D.,Hopkins, L.J.,Mirey, G.,Camonis, J.H.,Owen, D. (deposition date: 2003-03-05, release date: 2003-03-13, Last modification date: 2024-05-15)

Primary citation

Mott, H.R.,Nietlispach, D.,Hopkins, L.J.,Mirey, G.,Camonis, J.H.,Owen, D.
Structure of the GTPase-binding domain of Sec5 and elucidation of its Ral binding site.
J. Biol. Chem., 278:17053-17059, 2003

PubMed Abstract: The exocyst complex is involved in the final stages of exocytosis, when vesicles are targeted to the plasma membrane and dock. The regulation of exocytosis is vital for a number of processes, for example, cell polarity, embryogenesis, and neuronal growth formation. Regulation of the exocyst complex in mammals was recently shown to be dependent upon binding of the small G protein, Ral, to Sec5, a central component of the exocyst. This interaction is thought to be necessary for anchoring the exocyst to secretory vesicles. We have determined the structure of the Ral-binding domain of Sec5 and shown that it adopts a fold that has not been observed in a G protein effector before. This fold belongs to the immunoglobulin superfamily in a subclass known as IPT domains. We have mapped the Ral binding site on this domain and found that it overlaps with protein-protein interaction sites on other IPT domains but that it is completely different from the G protein-geranyl-geranyl interaction face of the Ig-like domain of the Rho guanine nucleotide dissociation inhibitor. This mapping, along with available site-directed mutagenesis data, allows us to predict how Ral and Sec5 may interact.

PubMed: 12624092
DOI: 10.1074/jbc.M300155200

Experimental method

SOLUTION NMR