Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein.
The cyclic GMP phosphodiesterase gamma-subunit (PDEgamma) was shown to belong to the family of natively unfolded proteins. Increasing temperature transforms the protein into a more ordered (but still relatively disordered) conformation. The C-terminal part of PDEgamma has a high-affinity zinc-binding site (Kd approximately 1 microM), with His75 and His79 being directly involved into the coordination of Zn2+. Zinc-loaded protein remains effectively unfolded. Possible implications of these findings to the functioning of PDEgamma are discussed.
Uversky
Vladimir N
VN
Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Russia. uversky@hydrogen.ucsc.edu
Permyakov
Sergey E
SE
Zagranichny
Vasily E
VE
Rodionov
Igor L
IL
Fink
Anthony L
AL
Cherskaya
Alexandra M
AM
Wasserman
Lyubov A
LA
Permyakov
Eugene A
EA
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000737:chemistry / Q000378:metabolism*; D020106:Acrylamide / Q000737:chemistry; D001665:Binding Sites; D002942:Circular Dichroism; D011485:Protein Binding; D011487:Protein Conformation; D020539:Sequence Analysis, Protein; D013050:Spectrometry, Fluorescence; D013696:Temperature; D015032:Zinc / Q000378:metabolism*
D020106:Acrylamide; D015106:3',5'-Cyclic-GMP Phosphodiesterases; D015032:Zinc