Ribose-5-phosphate isomerase: Difference between revisions

The structure of RpiA has been identified in many organisms including ''E. coli'' and ''Vibrio vulnificus''. The crystallized RpiA structure from both of these organisms is highly conserved in many respects. RpiA exists as a dimer with pseudo-2-fold symmetry, the interface of the dimer is composed of six different segments, which contain a number of interactions occurring between <scene name='Sandbox_Reserved_305/Alpha_helices/2'> α-helices </scene> and <scene name='Sandbox_Reserved_305/Beta_sheets/1'> β-sheets </scene>. Two salt bridges also link <scene name='44/446270/Cv/1'>Lys104 and Glu183</scene> of the same subunit. The <scene name='Sandbox_Reserved_305/Activesite/3'>RpiA and R5P complex</scene> occurs through the interaction between the ligand (R5P) and the following residues in the RpiA: <scene name='Sandbox_Reserved_305/Test/1'>Gly97, Asp84</scene>, Lys121, Lys7, Thr31 and Ser30. RpiA contains two sites for this interaction allowing two R5Ps to interact with one RpiA. The VvRpiA-R5P complex resembles the ''E. coli'' RpiA-A5P complex; however the VvRpiA-A5P complex reveals a different position than the R5P binding mode. The A5P interacts with the following residues: Asp8, Lys7, Ser30, Asp118 and Lys121.