New tools for carbohydrate sulfation analysis: heparan sulfate 2-O-sulfotransferase (HS2ST) is a target for small-molecule protein kinase inhibitors
New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors
Structure, interactions and action of Mycobacterium tuberculosis 3-hydroxyisobutyric acid dehydrogenase
Mutation of G51 in SepF impairs FtsZ assembly promoting ability of SepF and retards the division of Mycobacterium smegmatis cells
Stimulation of the ATPase activity of Hsp90 by zerumbone modification of its cysteine residues destabilizes its clients and causes cytotoxicity
Cartoon illustration of the simultaneous binding of PAP (a competitive inhibitor of the physiological enzyme co-factor adeonosine 3′-phosphate 5′-phosphosulfate, PAPS) and a heptapeptide saccharide substrate (sticks), poised for sulfation (dashed line) in the active site of heparan sulfate 2-O-sulfotransferase (PDB ID: 4NDZ). The PAP(S)-binding site and the oligosaccharide-binding sites provide dual opportunities for the screening, identification and rational design of small molecule inhibitors of this enzyme, which include the highly sulfated polyanionic drug suramin and the promiscuous protein kinase inhibitor rottlerin. Rottlerin competes with the PAPS co-factor in sulfotransferases, opening the door for the discovery and optimisation of other kinase inhibitors that inhibit these classes of enzyme, including protein tyrosine sulfotransferases (TPSTs). For further details, see the article by Byrne et al. in this issue (pages 2417–2433) and its companion article on pages 2435–2455. Image kindly provided by Neil Berry and Patrick Eyers.