2n78

Publication Abstract from PubMed

Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen and a primary cause of infection in humans. P. aeruginosa can acquire resistance against multiple groups of antimicrobial agents, including beta-lactams, aminoglycosides and fluoroquinolones, and multidrug resistance is increasing in this organism which makes treatment of the infections difficult and expensive. This has led to the unmet need for discovery of new compounds distinctly different from present antimicrobials. Protein synthesis is an essential metabolic process and a validated target for the development of new antibiotics. Translation initiation factor 1 from P. aeruginosa (Pa-IF1) is the smallest of the three initiation factors that acts to establish the 30S initiation complex to initiate translation during protein biosynthesis, and its structure is unknown. Here we report the 1H, 13C and 15N chemical shift assignments of Pa-IF1 as the basis for NMR structure determination and interaction studies. Secondary structure analyses deduced from the NMR chemical shift data have identified five beta-strands with an unusually extended beta-strand at the C-terminal end of the protein and one short alpha-helix arranged in the sequential order beta1-beta2-beta3-alpha1-beta4-beta5. This is further supported by 15N-{1H} hetero NOEs. These secondary structure elements suggest the Pa-IF1 adopts the typical beta-barrel structure and is composed of an oligomer-binding motif.

1H, 13C and 15N resonance assignments and secondary structure analysis of translation initiation factor 1 from Pseudomonas aeruginosa.,Bernal A, Hu Y, Palmer SO, Silva A, Bullard J, Zhang Y Biomol NMR Assign. 2016 Mar 16. PMID:26983940^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.