1oxz

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[[Image:1oxz.jpg|left|200px]]
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{{Structure
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|GENE= GGA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1oxz| PDB=1oxz | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxz OCA], [http://www.ebi.ac.uk/pdbsum/1oxz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oxz RCSB]</span>
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'''Crystal Structure of the Human GGA1 GAT domain'''
'''Crystal Structure of the Human GGA1 GAT domain'''
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[[Category: Zhang, X C.]]
[[Category: Zhang, X C.]]
[[Category: Zhu, G.]]
[[Category: Zhu, G.]]
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[[Category: gat domain]]
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[[Category: Gat domain]]
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[[Category: gga1]]
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[[Category: Gga1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:25:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:51:59 2008''
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Revision as of 01:25, 3 May 2008

Image:1oxz.jpg

Template:STRUCTURE 1oxz

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 Page seeded by OCA on Sat May 3 04:25:03 2008

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