title: (1)H, (13)C and (15)N resonance assignments and secondary structure analysis of translation initiation factor 1 from Pseudomonas aeruginosa.
abstract: 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 β-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 (1)H, (13)C and (15)N 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 β-strands with an unusually extended β-strand at the C-terminal end of the protein and one short α-helix arranged in the sequential order β1-β2-β3-α1-β4-β5. This is further supported by (15)N-{(1)H} hetero NOEs. These secondary structure elements suggest the Pa-IF1 adopts the typical β-barrel structure and is composed of an oligomer-binding motif.
authors.affiliation: Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA.
authors.forename: Alejandra
authors.initials: A
authors.lastname: Bernal
authors.affiliation: Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA.
authors.forename: Yanmei
authors.initials: Y
authors.lastname: Hu
authors.affiliation: Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA.
authors.forename: Stephanie O
authors.initials: SO
authors.lastname: Palmer
authors.affiliation: Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA.
authors.forename: Aaron
authors.initials: A
authors.lastname: Silva
authors.affiliation: Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA.
authors.forename: James
authors.initials: J
authors.lastname: Bullard
authors.affiliation: Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA. yonghong.zhang@utrgv.edu.
authors.forename: Yonghong
authors.identifier: 0000-0002-7305-9295
authors.initials: Y
authors.lastname: Zhang
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D039662:Prokaryotic Initiation Factors / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011550:Pseudomonas aeruginosa / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D039662:Prokaryotic Initiation Factors
keywords: NMR assignments; Protein secondary structure; Pseudomonas aeruginosa; Translation initiation factor 1 (IF1)