5AZW

Crystal structure of p24beta1 GOLD domain

Summary for 5AZW

• Entry DOI: 10.2210/pdb5azw/pdb
• Related: 5AZX 5AZY
• Descriptor: Transmembrane emp24 domain-containing protein 2, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: protein transport, gpi-anchored protein, p24 complex
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 21464.17

Authors

Nagae, M.,Yamaguchi, Y. (deposition date: 2015-10-23, release date: 2016-09-14, Last modification date: 2024-10-16)

Primary citation

Nagae, M.,Hirata, T.,Morita-Matsumoto, K.,Theiler, R.,Fujita, M.,Kinoshita, T.,Yamaguchi, Y.
3D Structure and Interaction of p24 beta and p24 delta Golgi Dynamics Domains: Implication for p24 Complex Formation and Cargo Transport
J.Mol.Biol., 428:4087-4099, 2016

PubMed Abstract: The p24 family consists of four subfamilies (p24α, p24β, p24γ, and p24δ), and the proteins are thought to form hetero-oligomeric complexes for efficient transport of cargo proteins from the endoplasmic reticulum to the Golgi apparatus. The proteins possess a conserved luminal Golgi dynamics (GOLD) domain, whose functions are largely unknown. Here, we present structural and biochemical studies of p24β1 and p24δ1 GOLD domains. Use of GOLD domain-deleted mutants revealed that the GOLD domain of p24δ1 is required for proper p24 hetero-oligomeric complex formation and efficient transport of GPI-anchored proteins. The p24β1 and p24δ1 GOLD domains share a common β-sandwich fold with a characteristic intrasheet disulfide bond. The GOLD domain of p24δ1 crystallized as dimers, allowing the analysis of a homophilic interaction site. Surface plasmon resonance and solution NMR analyses revealed that p24β1 and p24δ1 GOLD domains interact weakly (K= ~10M). Bi-protein titration provided interaction site maps. We propose that the heterophilic interaction of p24 GOLD domains contributes to the formation of the p24 hetero-oligomeric complex and to efficient cargo transport.

PubMed: 27569046
DOI: 10.1016/j.jmb.2016.08.023

Experimental method

X-RAY DIFFRACTION (1.5 Å)