The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families.

Bordo, D; Deriu, D; Colnaghi, R; Carpen, A; Pagani, S; Bolognesi, M

Bordo, D; Deriu, D; Colnaghi, R; Carpen, A; Pagani, S; Bolognesi, M.

Affiliation

Bordo D; Advanced Biotechnology Center, IST and Department of Physics, University of Genova INFM, Largo R. Benzi, 10, Genova, I-16132, Italy. bordo@alcor.cba.unige.it

J Mol Biol ; 298(4): 691-704, 2000 May 12.

Article in En | MEDLINE | ID: mdl-10788330

Subject(s)

Azotobacter vinelandii/enzymology; Evolution, Molecular; Phosphoric Monoester Hydrolases/chemistry; Sulfurtransferases/chemistry; Thiosulfate Sulfurtransferase/chemistry; Amino Acid Sequence; Animals; Binding Sites; Catalysis; Cattle; Crystallography, X-Ray; Humans; Hydrogen Bonding; Magnesium/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Alignment; Sequence Homology, Amino Acid; Static Electricity; Sulfurtransferases/genetics; Sulfurtransferases/metabolism; Water/metabolism

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Collection: 01-internacional Database: MEDLINE Main subject: Sulfurtransferases / Thiosulfate Sulfurtransferase / Azotobacter vinelandii / Phosphoric Monoester Hydrolases / Evolution, Molecular Limits: Animals / Humans Language: En Journal: J Mol Biol Year: 2000 Type: Article Affiliation country: Italy

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