Characterization of the proline-utilization pathway in Mycobacterium tuberculosis through structural and functional studies

The structure of Δ¹-pyrroline-5-carboxylic dehydrogenase (PruA), involved in proline utilization in M. tuberculosis, has been determined in apo and NAD⁺-bound forms. Opportunities for inhibitor development are identified and the proline-utilization pathway has been characterized with a novel use of NMR.

A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly

Two crystal structures of the major pilin SpaD from C. diphtheriae have been determined at 1.87 and 2.5 Å resolution. The N-terminal domain is found to contain an isopeptide bond that forms slowly over time in the recombinant protein. Given its structural context, this provides insight into the relationship between internal isopeptide-bond formation and pilus assembly.