1upt

From Proteopedia

Revision as of 15:03, 5 November 2007

STRUCTURE OF A COMPLEX OF THE GOLGIN-245 GRIP DOMAIN WITH ARL1

Overview

Golgins are large coiled-coil proteins that play a role in Golgi structure, and vesicle traffic. The Arf-like GTPase Arl1 regulates the translocation, of GRIP domain-containing golgins to Golgi membranes. We report here the, 1.7 A resolution structure of human Arl1-GTP in a complex with the GRIP, domain of golgin-245. The structure reveals that the GRIP domain consists, of an S-shaped arrangement of three helices. The domain forms a homodimer, that binds two Arl1-GTPs using two helices from each monomer. The, structure is consistent with golgin-245 forming parallel coiled-coils and, suggests how Arl1-GTP/GRIP complexes interact with Golgi membranes via the, N termini of Arl1-GTP and the C-terminal tails of the GRIP domains. In, cells, bivalent association with Arl1-GTP would increase residence time of, the golgins on Golgi membranes. Despite no conservation of sequence, topology, or even helical direction, several other effectors form similar, interactions with small GTPases via a pair of alpha helices, suggesting a, common structural basis for effector recognition.

About this Structure

1UPT is a Protein complex structure of sequences from Homo sapiens with MG and GTP as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus., Panic B, Perisic O, Veprintsev DB, Williams RL, Munro S, Mol Cell. 2003 Oct;12(4):863-74. PMID:14580338

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