Crystal Structures of Substrate and Inhibitor Complexes of Ribose 5-Phosphate Isomerase A from Vibrio vulnificus YJ016

  • Kim, Tae Gyun (Department of Chemistry, Pohang University of Science and Technology) ;
  • Kwon, Taek Hun (School of Life Sciences and Biotechnology, Korea University) ;
  • Min, Kyoungin (Department of Chemistry, Pohang University of Science and Technology) ;
  • Dong, Mi-Sook (School of Life Sciences and Biotechnology, Korea University) ;
  • Park, Young In (School of Life Sciences and Biotechnology, Korea University) ;
  • Ban, Changill (Department of Chemistry, Pohang University of Science and Technology)
  • Received : 2008.10.21
  • Accepted : 2008.10.28
  • Published : 2009.01.31


Ribose-5-phosphate isomerase A (RpiA) plays an important role in interconverting between ribose-5-phosphate (R5P) and ribulose-5-phosphate in the pentose phosphate pathway and the Calvin cycle. We have determined the crystal structures of the open form RpiA from Vibrio vulnificus YJ106 (VvRpiA) in complex with the R5P and the closed form with arabinose-5-phosphate (A5P) in parallel with the apo VvRpiA at $2.0{\AA}$ resolution. VvRpiA is highly similar to Escherichia coli RpiA, and the VvRpiA-R5P complex strongly resembles the E. coli RpiA-A5P complex. Interestingly, unlike the E. coli RpiA-A5P complex, the position of A5P in the VvRpiA-A5P complex reveals a different position than the R5P binding mode. VvRpiA-A5P has a sugar ring inside the binding pocket and a phosphate group outside the binding pocket: By contrast, the sugar ring of A5P interacts with the Asp4, Lys7, Ser30, Asp118, and Lys121 residues; the phosphate group of A5P interacts with two water molecules, W51 and W82.


Supported by : Pohang University of Science and Technology, Korea Health Industry Development Institute, Korea Health Industry Development Institute, Korea Research Foundation


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