1ZJ6

Crystal structure of human ARL5

Summary for 1ZJ6

• Entry DOI: 10.2210/pdb1zj6/pdb
• Descriptor: ADP-ribosylation factor-like protein 5, SULFATE ION, GUANOSINE-3'-MONOPHOSPHATE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: arl, gtp-binding, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 22539.39

Authors

Wang, Z.X.,Shi, L.,Liu, J.F.,An, X.M.,Chang, W.R.,Liang, D.C. (deposition date: 2005-04-28, release date: 2005-06-07, Last modification date: 2024-12-25)

Primary citation

Wang, Z.X.,Shi, L.,Liu, J.F.,An, X.M.,Chang, W.R.,Liang, D.C.
2.0A crystal structure of human ARL5-GDP3'P, a novel member of the small GTP-binding proteins
Biochem.Biophys.Res.Commun., 332:640-645, 2005

PubMed Abstract: ARL5 is a member of ARLs, which is widespread in high eukaryotes and homologous between species. But no structure or biological function of this member is reported. We expressed, purified, and resolved the structure of human ARL5 with bound GDP3'P at 2.0 A resolution. A comparison with the known structures of ARFs shows that besides the typical features of ARFs, human ARL5 has specific features of its own. Bacterially expressed human ARL5 contains bound GDP3'P which is seldom seen in other structures. The hydrophobic tail of the introduced detergent Triton X-305 binds at the possible myristoylation site of Gly2, simulating the myristoylated state of N-terminal amphipathic helix in vivo. The structural features of the nucleotide binding motifs and the switch regions prove that ARL5 will undergo the typical GDP/GTP structural cycle as other members of ARLs, which is the basis of their biological functions.

PubMed: 15896705
DOI: 10.1016/j.bbrc.2005.04.168

Experimental method

X-RAY DIFFRACTION (2 Å)