PDBsum entry: 1mhq

Protein transport

PDB id: 1mhq

Contents

Protein chains

143 a.a. *

Waters ×104

* Residue conservation analysis

PDB id:

1mhq

Name:

Protein transport

Title:

Crystal structure of human gga2 vhs domain

Structure:

Adp-ribosylation factor binding protein gga2. Chain: a, b. Fragment: vhs domain (n-terminal domain). Synonym: golgi-localized, gamma ear-containing, arf- binding protein 2. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.223 R-free: 0.267

Authors:

G.Zhu,X.C.Zhang

Key ref:

G.Zhu et al. (2003). Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket. FEBS Lett, 537, 171-176. PubMed id: 12606052 DOI: 10.1016/S0014-5793(03)00095-4

Date:

20-Aug-02 Release date: 11-Mar-03

Protein chains

Q9UJY4  (GGA2_HUMAN) -  ADP-ribosylation factor-binding protein GGA2

Seq: 613 a.a.

Struc: 143 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: intracellular protein transport (1 term)

DOI no: 10.1016/S0014-5793(03)00095-4

FEBS Lett 537:171-176 (2003)

PubMed id: 12606052

Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket.

G.Zhu, X.He, P.Zhai, S.Terzyan, J.Tang, X.C.Zhang.

ABSTRACT

Golgi-localized, gamma-ear-containing, ARF binding (GGA) proteins regulate intracellular vesicle transport by recognizing sorting signals on the cargo surface in the initial step of the budding process. The VHS (VPS27, Hrs, and STAM) domain of GGA binds with the signal peptides. Here, a crystal structure of the VHS domain of GGA2 is reported at 2.2 A resolution, which permits a direct comparison with that of homologous proteins, GGA1 and GGA3. Significant structural difference is present in the loop between helices 6 and 7, which forms part of the ligand binding pocket. Intrinsic fluorescence spectroscopic study indicates that this loop undergoes a conformational change upon ligand binding. Thus, the current structure suggests that a conformational change induced by ligand binding occurs in this part of the ligand pocket.

Selected figure(s)

Figure 1.
Fig. 1. Crystal structure of GGA2 VHS domain. a: A ribbon diagram with helices α1–α8 and the visible amino (N)- and carboxyl (C)-termini labeled. b: A molecular surface model in an orientation similar to a. Color coded are the amino acid residue conserveness of GGA2 compared with GGA1 and GGA3: white for identical to both, green for identical to either GGA1 or GGA3, and orange for different from both. c: The same as b but with a 180° rotation about the vertical axis. The ligand ACDL binding site, L[6,7] loop and visible N- and C-termini are labeled. This figure and Fig. 2 were drawn with programs MolScript, Raster3D or Grasp [27, 28 and 29].

Figure 3.
Fig. 3. Intrinsic fluorescence spectra of VHS/GGA2. Typical emission spectra of WT (top) and W122R mutant (bottom) of VHS/GGA2 in the absence (solid line) and presence (dashed line) of the CI-MPR peptide are shown, which suggest that GGA2 Trp^122 was subjected to an environmental change upon ligand binding. Fluorescence intensities are shown in an arbitrary unit.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2003, 537, 171-176) copyright 2003.

Figures were selected by an automated process.