4ZI2

BART-like domain of BARTL1/CCDC104 in complex with Arl3FL bound to GppNHp in P21 21 21

Summary for 4ZI2

• Entry DOI: 10.2210/pdb4zi2/pdb
• Descriptor: ADP-ribosylation factor-like protein 3, Cilia- and flagella-associated protein 36, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• Functional Keywords: complex, arf-like gtpase, gtp-binding, bart-like domain, cilia, hydrolase
• Biological source: Mus musculus (House Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 75399.35

Authors

Lokaj, M.,Koerner, C.,Koesling, S.,Wittinghofer, A. (deposition date: 2015-04-27, release date: 2015-11-11, Last modification date: 2024-01-10)

Primary citation

Lokaj, M.,Kosling, S.K.,Koerner, C.,Lange, S.M.,van Beersum, S.E.,van Reeuwijk, J.,Roepman, R.,Horn, N.,Ueffing, M.,Boldt, K.,Wittinghofer, A.
The Interaction of CCDC104/BARTL1 with Arl3 and Implications for Ciliary Function.
Structure, 23:2122-2132, 2015

PubMed Abstract: Cilia are small antenna-like cellular protrusions critical for many developmental signaling pathways. The ciliary protein Arl3 has been shown to act as a specific release factor for myristoylated and farnesylated ciliary cargo molecules by binding to the effectors Unc119 and PDE6δ. Here we describe a newly identified Arl3 binding partner, CCDC104/CFAP36. Biochemical and structural analyses reveal that the protein contains a BART-like domain and is called BARTL1. It recognizes an LLxILxxL motif at the N-terminal amphipathic helix of Arl3, which is crucial for the interaction with the BART-like domain but also for the ciliary localization of Arl3 itself. These results seem to suggest a ciliary role of BARTL1, and possibly link it to the Arl3 transport network. We thus speculate on a regulatory mechanism whereby BARTL1 aids the presentation of active Arl3 to its GTPase-activating protein RP2 or hinders Arl3 membrane binding in the area of the transition zone.

PubMed: 26455799
DOI: 10.1016/j.str.2015.08.016

Experimental method

X-RAY DIFFRACTION (2.2 Å)