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

FEBS Letters

Zhang, Xuejun C.¹  Tang, Jordan²  Terzyan, Simon¹  He, Xiangyuan²  Zhai, Peng¹  Zhu, Guangyu¹ 

[1] Crystallography Research Program of Oklahoma Medical Research Foundation, 825 N.E. 13th Street, Oklahoma City, OK 73104, USA;Protein Studies Program of Oklahoma Medical Research Foundation, 825 N.E. 13th Street, Oklahoma City, OK 73104, USA

关键词: VPS27;    Hrs;    and STAM domain;    Golgi-localized γ-ear-containing ARF binding protein;    Ligand binding;    Crystal structure;    Intrinsic fluorescence spectroscopy;    GGA;    Golgi-localized;    γ-ear-containing;    ARF binding protein;    VHS;    VPS27;    Hrs;    and STAM domain;    TGN;    trans-Golgi network;    MPR;    mannose-6-phosphate receptor;    ACDL;    acidic cluster-dileucine;    WT;    wild-type;    CI-MPR;    cation-independent-MPR;    rmsd;    root mean square deviation;   

DOI  :  10.1016/S0014-5793(03)00095-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Golgi-localized, γ-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 Å 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.

【 授权许可】

Unknown