2A2F

Crystal Structure of Sec15 C-terminal domain

Summary for 2A2F

• Entry DOI: 10.2210/pdb2a2f/pdb
• Descriptor: Exocyst complex component Sec15 (2 entities in total)
• Functional Keywords: all helical structure, protein transport
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 37961.69

Authors

Wu, S.,Mehta, S.Q.,Pichaud, F.,Bellen, H.J.,Quiocho, F.A. (deposition date: 2005-06-22, release date: 2005-09-13, Last modification date: 2024-02-14)

Primary citation

Wu, S.,Mehta, S.Q.,Pichaud, F.,Bellen, H.J.,Quiocho, F.A.
Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo.
Nat.Struct.Mol.Biol., 12:879-885, 2005

PubMed Abstract: Sec15, a component of the exocyst, recognizes vesicle-associated Rab GTPases, helps target transport vesicles to the budding sites in yeast and is thought to recruit other exocyst proteins. Here we report the characterization of a 35-kDa fragment that comprises most of the C-terminal half of Drosophila melanogaster Sec15. This C-terminal domain was found to bind a subset of Rab GTPases, especially Rab11, in a GTP-dependent manner. We also provide evidence that in fly photoreceptors Sec15 colocalizes with Rab11 and that loss of Sec15 affects rhabdomere morphology. Determination of the 2.5-A crystal structure of the C-terminal domain revealed a novel fold consisting of ten alpha-helices equally distributed between two subdomains (N and C subdomains). We show that the C subdomain, mainly via a single helix, is sufficient for Rab binding.

PubMed: 16155582
DOI: 10.1038/nsmb987

Experimental method

X-RAY DIFFRACTION (2.5 Å)