1oxz

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Revision as of 16:31, 12 November 2007

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spinqualitylabelsall models 1oxz, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the Human GGA1 GAT domain

Overview

GGAs are a family of vesicle-coating regulatory proteins that function in, intracellular protein transport. A GGA molecule contains four domains, each mediating interaction with other proteins in carrying out, intracellular transport. The GAT domain of GGAs has been identified as the, structural entity that binds membrane-bound ARF, a molecular switch, regulating vesicle-coat assembly. It also directly interacts with, rabaptin5, an essential component of endosome fusion. A 2.8 A resolution, crystal structure of the human GGA1 GAT domain is reported here. The GAT, domain contains four helices and has an elongated shape with the longest, dimension exceeding 80 A. Its longest helix is involved in two structural, motifs: an N-terminal helix-loop-helix motif and a C-terminal three-helix, bundle. The N-terminal motif harbors the most conservative amino acid, sequence in the GGA GAT domains. Within this conserved region, a cluster, of residues previously implicated in ARF binding forms a hydrophobic, surface patch, which is likely to be the ARF-binding site. In addition, a, structure-based mutagenesis-biochemical analysis demonstrates that the, C-terminal three-helix bundle of this GAT domain is responsible for the, rabaptin5 binding. These structural characteristics are consistent with a, model supporting multiple functional roles for the GAT domain.

About this Structure

1OXZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human GGA1 GAT domain., Zhu G, Zhai P, He X, Terzyan S, Zhang R, Joachimiak A, Tang J, Zhang XC, Biochemistry. 2003 Jun 3;42(21):6392-9. PMID:12767220

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