4P34

Crystal structure of DJ-1 in sulfenic acid form (fresh crystal)

Summary for 4P34

• Entry DOI: 10.2210/pdb4p34/pdb
• Related: 4P2G 4P35 4P36
• Descriptor: Protein DJ-1, PENTAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: parkinson's disease, sufenic acid oxidation, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Cell membrane ; Lipid-anchor : Q99497
• Total number of polymer chains: 1
• Total formula weight: 20171.33

Authors

Tashiro, S.,Wu, C.-X.,Hoang, Q.Q.,Caaveiro, J.M.M.,Tsumoto, K. (deposition date: 2014-03-05, release date: 2014-04-09, Last modification date: 2023-11-15)

Primary citation

Tashiro, S.,Caaveiro, J.M.,Wu, C.X.,Hoang, Q.Q.,Tsumoto, K.
Thermodynamic and Structural Characterization of the Specific Binding of Zn(II) to Human Protein DJ-1.
Biochemistry, 53:2218-2220, 2014

PubMed Abstract: Mutations of DJ-1 cause familial Parkinson's disease (PD), although the role of DJ-1 in PD remains unresolved. Very recent reports have shown that DJ-1 interacts with copper ions. This evidence opens new avenues to understanding the function of DJ-1 and its role in PD. Herein, we report that Zn(II) binds to DJ-1 with great selectivity among the other metals examined: Mn(II), Fe(II), Co(II), Ni(II), and Cu(II). High-resolution X-ray crystallography (1.18 Å resolution) shows Zn(II) is coordinated to the protein by the key residues Cys106 and Glu18. These results suggest that DJ-1 may be regulated and/or stabilized by Zn(II).

PubMed: 24697266
DOI: 10.1021/bi500294h

Experimental method

X-RAY DIFFRACTION (1.55 Å)