title: Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus.
abstract: Thiaminase type II (TenA) catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus (Sa). SaTenA was crystallized by the vapour-diffusion method and the resulting crystal diffracted to 2.6 Å resolution usng synchrotron radiation. The crystal is orthorhombic, belonging to space group P2(1)2(1)2(1) with unit-cell parameters a=103.5, b=104.1, c=109.6 Å. With four molecules in the asymmetric unit, the Matthews coefficient is 2.85 Å3 Da(-1). Initial attempts to solve the structure by molecular-replacement techniques were successful.
authors.affiliation: Laboratory for Structural Biology of Infection and Inflammation, University of Hamburg, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Afshan
authors.initials: A
authors.lastname: Begum
authors.forename: Julia
authors.initials: J
authors.lastname: Drebes
authors.forename: Markus
authors.initials: M
authors.lastname: Perbandt
authors.forename: Carsten
authors.initials: C
authors.lastname: Wrenger
authors.forename: Christian
authors.initials: C
authors.lastname: Betzel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D006867:Hydrolases; C022731:thiaminase II