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4ZI3

BART-like domain of BARTL1/CCDC104 aa1-133 in complex with Arl3FL bound to GppNHp in P1 21 1

Summary for 4ZI3
Entry DOI10.2210/pdb4zi3/pdb
DescriptorADP-ribosylation factor-like protein 3, Cilia- and flagella-associated protein 36, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (6 entities in total)
Functional Keywordsarf-like gtpase, gtp-binding, bart-like domain, cilia, hydrolase
Biological sourceMus musculus (House Mouse)
More
Cellular locationGolgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side: Q9WUL7
Nucleus : Q8C6E0 Q8C6E0
Total number of polymer chains4
Total formula weight75245.18
Authors
Lokaj, M.,Koerner, C.,Koesling, S.,Wittinghofer, A. (deposition date: 2015-04-27, release date: 2016-03-23, Last modification date: 2024-01-10)
Primary citationLokaj, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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