1MI1

Crystal Structure of the PH-BEACH Domain of Human Neurobeachin

Summary for 1MI1

• Entry DOI: 10.2210/pdb1mi1/pdb
• Descriptor: Neurobeachin (1 entity in total)
• Functional Keywords: ph domain, beach domain, vesicle trafficking, signal transduction, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q8NFP9
• Total number of polymer chains: 2
• Total formula weight: 96433.81

Authors

Jogl, G.,Shen, Y.,Gebauer, D.,Li, J.,Wiegmann, K.,Kashkar, H.,Kroenke, M.,Tong, L.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2002-08-21, release date: 2002-09-27, Last modification date: 2024-11-20)

Primary citation

Jogl, G.,Shen, Y.,Gebauer, D.,Li, J.,Wiegmann, K.,Kashkar, H.,Kronke, M.,Tong, L.
Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain.
EMBO J., 21:4785-4795, 2002

PubMed Abstract: The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures. Unexpectedly, the structure also reveals that the BEACH domain is in extensive association with a novel, weakly conserved pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong interactions, suggesting they may function as a single unit. Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners.

PubMed: 12234919
DOI: 10.1093/emboj/cdf502

Experimental method

X-RAY DIFFRACTION (2.9 Å)