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1KSH

Complex of Arl2 and PDE delta, Crystal Form 2 (native)

Summary for 1KSH
Entry DOI10.2210/pdb1ksh/pdb
Related1KSG 1KSJ 1doa 1fzq
Descriptorarf-like protein 2, RETINAL ROD RHODOPSIN-SENSITIVE CGMP 3',5'-CYCLIC PHOSPHODIESTERASE DELTA-SUBUNIT, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordssmall gtpase, small gtp-binding protein, arf family, effector molecule, immunoglobuline-like fold, gdi, signaling protein-hydrolase complex, signaling protein/hydrolase
Biological sourceMus musculus (house mouse)
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Cellular locationMitochondrion intermembrane space: Q9D0J4
Total number of polymer chains2
Total formula weight39333.89
Authors
Hanzal-Bayer, M.,Renault, L.,Roversi, P.,Wittinghofer, A.,Hillig, R.C. (deposition date: 2002-01-13, release date: 2002-05-08, Last modification date: 2024-11-06)
Primary citationHanzal-Bayer, M.,Renault, L.,Roversi, P.,Wittinghofer, A.,Hillig, R.C.
The complex of Arl2-GTP and PDE delta: from structure to function.
EMBO J., 21:2095-2106, 2002
Cited by
PubMed Abstract: Arf-like (Arl) proteins are close relatives of the Arf regulators of vesicular transport, but their function is unknown. Here, we present the crystal structure of full-length Arl2-GTP in complex with its effector PDE delta solved in two crystal forms (Protein Data Bank codes 1KSG, 1KSH and 1KSJ). Arl2 shows a dramatic conformational change from the GDP-bound form, which suggests that it is reversibly membrane associated. PDE delta is structurally closely related to RhoGDI and contains a deep empty hydrophobic pocket. Further experiments show that H-Ras, Rheb, Rho6 and G alpha(i1) interact with PDE delta and that, at least for H-Ras, the intact C-terminus is required. We suggest PDE delta to be a specific soluble transport factor for certain prenylated proteins and Arl2-GTP a regulator of PDE delta-mediated transport.
PubMed: 11980706
DOI: 10.1093/emboj/21.9.2095
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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数据于2025-07-30公开中

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