NDLI: Role of Pyridoxal 5′-Phosphate in the Structural Stabilization of O-Acetylserine Sulfhydrylase

Content Provider	Journal of Biological Chemistry (JBC)
Author	Bettati, Stefano Benci, Sara Campanini, Barbara Raboni, Samanta Chirico, Giuseppe Beretta, Sabrina Schnackerz, Klaus D. Hazlett, Theodore L. Gratton, Enrico Mozzarelli, Andrea
Abstract	Proteins belonging to the superfamily of pyridoxal 5′-phosphate-dependent enzymes are currently classified into three functional groups and five distinct structural fold types. The variation within this enzyme group creates an ideal system to investigate the relationships among amino acid sequences, folding pathways, and enzymatic functions. The number of known three-dimensional structures of pyridoxal 5′-phosphate-dependent enzymes is rapidly increasing, but only for relatively few have the folding mechanisms been characterized in detail. The dimeric O-acetylserine sulfhydrylase fromSalmonella typhimurium belongs to the β-family and fold type II group. Here we report the guanidine hydrochloride-induced unfolding of the apo- and holoprotein, investigated using a variety of spectroscopic techniques. Data from absorption, fluorescence, circular dichroism, 31P nuclear magnetic resonance, time-resolved fluorescence anisotropy, and photon correlation spectroscopy indicate that the O-acetylserine sulfhydrylase undergoes extensive disruption of native secondary and tertiary structure before monomerization. Also, we have observed that the holo-O-acetylserine sulfhydrylase exhibits a greater conformational stability than the apoenzyme form. The data are discussed in light of the fact that the role of the coenzyme in structural stabilization varies among the pyridoxal 5′-phosphate-dependent enzymes and does not seem to be linked to the particular enzyme fold type.
Related Links	http://www.jbc.org/content/275/51/40244.abstract
Ending Page	40251
Starting Page	40244
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	51
Volume Number	275
DOI	10.1074/jbc.M007015200
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2000-12-22
Access Restriction	Open
Subject Keyword	Pyridoxal 5′-phosphate (PLP) O-acetylserine sulfhydrylase (OASS) Guanidinium hydrochloride (GdnHCl) Bis-tris[bis-(2-hydroxyethyl)imino]-tris[(hydroxymethyl)propane] (Bis-Tris propane) Nuclear magnetic resonance (NMR) 2-(N-morpholino)ethanesulphonic acid (MES) PROTEIN STRUCTURE AND FOLDING
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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