1KSJ: Complex Of Arl2 And Pde Delta, Crystal Form 2 (semet)

Citation:
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.
PDB ID: 1KSJDownload
MMDB ID: 71321
PDB Deposition Date: 2002/1/13
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Mus musculus
Similar Structures:
Biological Unit for 1KSJ: dimeric; determined by author
Molecular Components in 1KSJ
Label Count Molecule
Proteins (2 molecules)
1
Arf-like Protein 2(Gene symbol: Arl2)
Molecule annotation
1
Retinal ROD Rhodopsin-sensitive Cgmp 3',5'-cyclic Phosphodiesterase Delta-subunit(Gene symbol: PDE6D)
Molecule annotation
Chemicals (5 molecules)
1
1
2
1
3
1
4
1
5
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.