Apo and substrate-bound dihydropteroate synthase crystal structures from Thermus thermophilus HB8.
High-resolution crystal structures of Thermus thermophilus HB8 DHPS and homologs from Escherichia coli and Mycobacterium tuberculosis highlight conserved catalytic features, as well as variable loop conformations and phosphate-binding residues that may contribute to differential sulfonamide sensitivity.