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Articles by S Fujii
Total Records ( 2 ) for S Fujii
  H Ikushiro , M. M Islam , A Okamoto , J Hoseki , T Murakawa , S Fujii , I Miyahara and H. Hayashi
 

Serine palmitoyltransferase (SPT) is a key enzyme of sphingolipid biosynthesis and catalyses the pyridoxal 5'-phosphate (PLP)-dependent decarboxylative condensation reaction of l-serine with palmitoyl-CoA to generate 3-ketodihydrosphingosine. The crystal structure of SPT from Sphingobacterium multivorum GTC97 complexed with l-serine was determined at 2.3 Å resolution. The electron density map showed the Schiff base formation between l-serine and PLP in the crystal. Because of the hydrogen bond formation with His138, the orientation of the C–H bond of the PLP–l-serine aldimine was not perpendicular to the PLP–Schiff base plane. This conformation is unfavourable for the -proton abstraction by Lys244 and the reaction is expected to stop at the PLP–l-serine aldimine. Structural modelling of the following intermediates indicated that His138 changes its hydrogen bond partner from the carboxyl group of l-serine to the carbonyl group of palmitoyl-CoA upon the binding of palmitoyl-CoA, making the l-serine C–H bond perpendicular to the PLP–Schiff base plane. These crystal and model structures well explained the observations on bacterial SPTs that the -deprotonation of l-serine occurs only in the presence of palmitoyl-CoA. This study provides the structural evidence that directly supports our proposed mechanism of the substrate synergism in the SPT reaction.

  T Takahashi , H Satoh , M Takaguchi , S Takafuji , H Yokoyama , S Fujii and T. Suzuki
 

Association of sulphatide with influenza A virus (IAV) haemagglutinin (HA) delivered to the cell surface promotes progeny virus production. However, it is not known whether there is direct binding of HA to sulphatide. In this study, we found that recombinant HA, which was produced by a baculovirus protein expression system from the HA gene of A/duck/HK/313/4/78 (H5N3), bound to sulphatide in a dose-dependent manner and that the binding was inhibited by a specific antibody. Our results indicate that the recombinant HA is useful for elucidation of the binding domain of HA with sulphatide and for the development of new anti-IAV agents.

 
 
 
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