The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate
substrates of GroEL share the (βα) 8 TIM-barrel fold, but how the chaperonin promotes …

Enzymes are usually comprised of multiple subunits and more often than not they are made
up of identical subunits. In this review we examine lysine biosynthesis and focus on the …

Many proteins assemble into homomultimeric structures, with a number of subunits that can
vary substantially among phylogenetic lineages. As protein-protein interactions require …

Dihydrodipicolinate synthase (DHDPS) catalyzes the rate limiting step in lysine biosynthesis
in bacteria and plants. The structure of DHDPS has been determined from several bacterial …

Given the rise in drug-resistant Streptococcus pneumoniae, there is an urgent need to
discover new antimicrobials targeting this pathogen and an equally urgent need to …

Dihydrodipicolinate synthase (DHDPS), an enzyme of the meso-diaminopimelate pathway
of lysine biosynthesis, is essential for bacterial growth and is considered a target for novel …

Given the emergence of multi drug resistant Vibrio cholerae strains, there is an urgent need
to characterize new anti-cholera targets. One such target is the enzyme dihydrodipicolinate …

The metal-dependent M17 aminopeptidases are conserved throughout all kingdoms of life.
This large enzyme family is characterized by a conserved binuclear metal center and a …

Many proteins adopt homomeric quaternary structures to support their biological function,
including the first enzyme of the shikimate pathway that is ultimately responsible for the …

Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step in the
diaminopimelate pathway of bacteria, yielding amino acids required for cell wall and protein …