Structural highlights
Publication Abstract from PubMed
Ribose is transported into cells in its pyranose form and must be rearranged to its furanose form for further utilization. Ribose pyranase RbsD catalyzes the conversion of ribose from the pyranose to furanose form. This is the key step for substrate supply to ribokinase RbsK, which converts ribose to ribose-5-phosphate for further metabolism. Sequence analysis indicated Sa240 from Staphylococcus aureus was a ribose pyranase homolog. Here we showed that Sa240 formed dimeric structure both in solution and in crystal. S240-ribose complex structure showed a ribose binding site formed by an incomplete active site compared with RbsD. Because the catalytic activity of ribose pyranase depends on its oligomeric state, we propose Sa240 is catalytically inactive in its dimeric structure.
Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus.,Wang L, Wu M, Zang J J Struct Biol. 2011 May;174(2):413-9. Epub 2011 Jan 27. PMID:21276853[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang L, Wu M, Zang J. Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus. J Struct Biol. 2011 May;174(2):413-9. Epub 2011 Jan 27. PMID:21276853 doi:10.1016/j.jsb.2011.01.007
