Crystallization and preliminary X-ray diffraction studies of mammalian purple acid phosphatase.
نویسندگان
چکیده
The oxidized form of purple acid phosphatase from pig allantoic fluid has been crystallized in the presence of phosphate using the hanging-drop technique. The crystals belong to the space group P2(1)2(1)2(1) and have unit-cell parameters a = 66.8, b = 70.3, c = 78.7 A. Diffraction data collected from a cryocooled crystal using a conventional X-ray source extend to 1.55 A resolution. A knowledge of the three-dimensional structure of mammalian purple acid phosphatase will aid in understanding the substrate specificity of the enzyme and will be important in the rational design of inhibitors, with potential in the treatment of bone diseases.
منابع مشابه
Purification, crystallization and preliminary X-ray diffraction studies of recombinant class A non-specific acid phosphatase of Salmonella typhimurium.
The phoN gene of Salmonella enterica sv. Typhimurium strain MD6001 was cloned in the multicopy plasmid pBluescript SK(-). The nucleotide sequence of the cloned gene differs from the corresponding S. typhimurium LT2 sequence at 23 residues, leading to 15 amino-acid differences, but was very close to the S. typhi phoN sequence (only three nucleotide and two amino-acid differences). The recombinan...
متن کاملAmino Acid Composition, Crystallization and Preliminary X-ray Diffraction Studies of Guanylonbonuclease from Streptomyces Aureofaciens
The amino acid composition and preparation of crystals for X ray diffraction analysis of guanylonbonuclease isolated from Streptomyces aureofa ciens is described. Single crystals have been grown from ammonium sulphate solutions. The crystals are orthorombic, space group P 2i2]2, cell dimmensions a = 6.47 nm, b = 7.89 nm, c = 3.93 nm. There are two molecules of a molecular weight of 10 600 in t...
متن کاملPurification, crystallization and preliminary X-ray crystallographic analysis of the phosphatase domain (PA3346PD) of the response regulator PA3346 from Pseudomonas aeruginosa PAO1.
The phosphatase domain (PA3346PD) of the response regulator PA3346 modulates the downstream anti-anti-σ factor PA3347 to regulate swarming motility in Pseudomonas aeruginosa PAO1. PA3346PD, which comprises the protein phosphatase 2C domain (PP2C), is classified as a Ser/Thr phosphatase of the Mg(2+)- or Mn(2+)-dependent protein phosphatase (PPM) family. The recombinant PA3346PD, with molecular ...
متن کاملExpression, purification, crystallization and preliminary X-ray diffraction analysis of a mammalian type 10 adenylyl cyclase.
The second messenger cAMP is synthesized in mammals by ten differently regulated adenylyl cyclases (AC1-10). These ACs are grouped into nucleotidyl cyclase class III based on homologies in their catalytic domains. The catalytic domain of AC10 is unique, however, in being activated through direct interaction with calcium and bicarbonate. Here, the production, crystallization and X-ray diffractio...
متن کاملNeutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase.
The enzyme 2-keto-3-deoxy-9-O-phosphonononic acid phosphatase (KDN9P phosphatase) functions in the pathway for the production of 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid, a sialic acid that is important for the survival of commensal bacteria in the human intestine. The enzyme is a member of the haloalkanoate dehalogenase superfamily and represents a good model for the active-site protona...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Acta crystallographica. Section D, Biological crystallography
دوره 55 Pt 8 شماره
صفحات -
تاریخ انتشار 1999