1R4A

Crystal Structure of GTP-bound ADP-ribosylation Factor Like Protein 1 (Arl1) and GRIP Domain of Golgin245 COMPLEX

Summary for 1R4A

• Entry DOI: 10.2210/pdb1r4a/pdb
• Descriptor: ADP-ribosylation factor-like protein 1, Golgi autoantigen, golgin subfamily A member 4, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: ras-like g protein structure, three-helix grip domain, protein transport
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side: P61212; Cytoplasm: Q13439
• Total number of polymer chains: 8
• Total formula weight: 101929.56

Authors

Wu, M.,Lu, L.,Hong, W.,Song, H. (deposition date: 2003-10-04, release date: 2004-01-13, Last modification date: 2023-10-25)

Primary citation

Wu, M.,Lu, L.,Hong, W.,Song, H.
Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1.
Nat.Struct.Mol.Biol., 11:86-94, 2004

PubMed Abstract: Recruitment of the GRIP domain golgins to the trans-Golgi network is mediated by Arl1, a member of the ARF/Arl small GTPase family, through interaction between their GRIP domains and Arl1-GTP. The crystal structure of Arl1-GTP in complex with the GRIP domain of golgin-245 shows that Arl1-GTP interacts with the GRIP domain predominantly in a hydrophobic manner, with the switch II region conferring the main recognition surface. The involvement of the switch and interswitch regions in the interaction between Arl1-GTP and GRIP accounts for the specificity of GRIP domain for Arl1-GTP. Mutations that abolished the Arl1-mediated Golgi localization of GRIP domain golgins have been mapped on the interface between Arl1-GTP and GRIP. Notably, the GRIP domain forms a homodimer in which each subunit interacts separately with one Arl1-GTP. Mutations disrupting the GRIP domain dimerization also abrogated its Golgi targeting, suggesting that the dimeric form of GRIP domain is a functional unit.

PubMed: 14718928
DOI: 10.1038/nsmb714

Experimental method

X-RAY DIFFRACTION (2.3 Å)