1oxz
From Proteopedia
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==Overview== | ==Overview== | ||
| - | GGAs are a family of vesicle-coating regulatory proteins that function in | + | 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== | ==About this Structure== | ||
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[[Category: Zhai, P.]] | [[Category: Zhai, P.]] | ||
[[Category: Zhang, R.]] | [[Category: Zhang, R.]] | ||
| - | [[Category: Zhang, X | + | [[Category: Zhang, X C.]] |
[[Category: Zhu, G.]] | [[Category: Zhu, G.]] | ||
[[Category: gat domain]] | [[Category: gat domain]] | ||
[[Category: gga1]] | [[Category: gga1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:54 2008'' |
Revision as of 12:22, 21 February 2008
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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 Thu Feb 21 14:22:54 2008
Categories: Homo sapiens | Single protein | He, X. | Joachimiak, A. | Tang, J. | Terzyan, S. | Zhai, P. | Zhang, R. | Zhang, X C. | Zhu, G. | Gat domain | Gga1
