3ENW
Substrate and inhibitor complexes of ribose 5-phosphate isomerase from Vibrio vulnificus YJ016
Summary for 3ENW
| Entry DOI | 10.2210/pdb3enw/pdb |
| Related | 3ENV |
| Descriptor | Ribose-5-phosphate isomerase A, RIBULOSE-5-PHOSPHATE (3 entities in total) |
| Functional Keywords | ribose 5-phosphate, arabinose 5-phosphate, isomerase |
| Biological source | Vibrio vulnificus |
| Total number of polymer chains | 2 |
| Total formula weight | 49804.65 |
| Authors | Min, K.,Kwon, T.H.,Kim, T.G. (deposition date: 2008-09-26, release date: 2009-09-29, Last modification date: 2023-11-01) |
| Primary citation | Kim, T.G.,Kwon, T.H.,Min, K.,Dong, M.S.,Park, Y.I.,Ban, C. Crystal structures of substrate and inhibitor complexes of ribose 5-phosphate isomerase A from Vibrio vulnificus YJ016 Mol.Cells, 27:99-103, 2009 Cited by PubMed Abstract: 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 A resolution. VvRpiA is highly similar to Eschericihia coliRpiA, 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. PubMed: 19214439DOI: 10.1007/s10059-009-0010-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
