Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):51-3. doi: 10.1107/S1744309110043174. Epub 2010 Dec 21.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification*
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Hydrolases / isolation & purification*
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Alignment
  • Staphylococcus aureus / enzymology*

Substances

  • Bacterial Proteins
  • Hydrolases
  • thiaminase II