Homology modeling of putative thioredoxin<i style=""> </i>from <i style="">Helicobacetr pylori</i>

Abstract

The tertiary structure of putative thioredoxin (trx) of <i style="">Helicobacter pylori</i> was generated based on structural homology of the X-ray crystallographic structure of thioredoxin from <i style="">Escherichia coli</i>. Inspection of theoretically predicted structure indicates that the thioredoxin of <i style="">H. pylori</i> is similar to that of <i style="">E. coli</i>. Analysis of the structure revealed that thioredoxins have a common fold, characterized by a core of twisted β-pleated sheet flanked either side by helices. The amino terminal end of the molecule is occupied by β-<img src='/image/spc_char/alpha.gif'>-β motif and carboxy terminal end by β-β-<img src='/image/spc_char/alpha.gif'> motif. This molecule is characterized by five strands and four helices. Among the four helices, <img src='/image/spc_char/alpha.gif'>₂ is the longest helix which was disrupted near proline. Proline72 is identified as <i style="">cis</i>-proline. This structure retained overall trx-fold with the conservation of global shape and the secondary structures. This work determines the structure of thioredoxin and is found to be unique for further insight into molecular characterization.