Mowbray, Sherry
- Institutionen för molekylär biovetenskap, Sveriges lantbruksuniversitet
Sammanfattning
Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 Angstrom resolution (R factor 22.4%, R-free 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 Angstrom resolution. A mechanism for acid-base catalysis is proposed
Publicerad i
Structure
2003, volym: 11, nummer: 1, sidor: 31-42
Utgivare: CELL PRESS
SLU författare
UKÄ forskningsämne
Veterinärmedicin
Husdjursvetenskap
Livsmedelsvetenskap
Publikationens identifierare
- DOI: https://doi.org/10.1016/S0969-2126(02)00933-4
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/835