3P12

Crystal Structure of D-ribose Pyranase Sa240

Summary for 3P12

• Entry DOI: 10.2210/pdb3p12/pdb
• Related: 3P13
• Descriptor: D-ribose pyranase, GLYCEROL (3 entities in total)
• Functional Keywords: rbsd, d-ribose pyranase, sa240, carbohydrate metabolism, isomerase
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm (Potential): Q2G1A5
• Total number of polymer chains: 4
• Total formula weight: 66143.74

Authors

Wu, M.,Wang, L.,Zang, J. (deposition date: 2010-09-29, release date: 2011-05-25, Last modification date: 2024-03-20)

Primary citation

Wang, L.,Wu, M.,Zang, J.
Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus
J.Struct.Biol., 174:413-419, 2011

PubMed Abstract: 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.

PubMed: 21276853
DOI: 10.1016/j.jsb.2011.01.007

Experimental method

X-RAY DIFFRACTION (2.35 Å)