7T50

Crystal structure of the molybdate-binding periplasmic protein ModA from the bacteria Pseudomonsa aeruginosa in chromate-bound form

Summary for 7T50

• Entry DOI: 10.2210/pdb7t50/pdb
• Related: 7T4Z
• Descriptor: Molybdate-binding periplasmic protein ModA, Chromate, AMMONIUM ION, ... (5 entities in total)
• Functional Keywords: molybdate-binding periplasmic protein, metal binding protein
• Biological source: Pseudomonas aeruginosa PA1
• Total number of polymer chains: 2
• Total formula weight: 49413.38

Authors

Ngu, D.H.Y.,Luo, Z.,Lim, B.Y.J.,Kobe, B. (deposition date: 2021-12-11, release date: 2022-05-04, Last modification date: 2023-10-18)

Primary citation

Maunders, E.A.,Ngu, D.H.Y.,Ganio, K.,Hossain, S.I.,Lim, B.Y.J.,Leeming, M.G.,Luo, Z.,Tan, A.,Deplazes, E.,Kobe, B.,McDevitt, C.A.
The Impact of Chromate on Pseudomonas aeruginosa Molybdenum Homeostasis.
Front Microbiol, 13:903146-903146, 2022

PubMed Abstract: Acquisition of the trace-element molybdenum the high-affinity ATP-binding cassette permease ModABC is essential for respiration in anaerobic and microaerophilic environments. This study determined the X-ray crystal structures of the molybdenum-recruiting solute-binding protein ModA from PAO1 in the metal-free state and bound to the group 6 metal oxyanions molybdate, tungstate, and chromate. PAO1 ModA has a non-contiguous dual-hinged bilobal structure with a single metal-binding site positioned between the two domains. Metal binding results in a 22° relative rotation of the two lobes with the oxyanions coordinated by four residues, that contribute six hydrogen bonds, distinct from ModA orthologues that feature an additional oxyanion-binding residue. Analysis of 485 ModA sequences revealed conservation of the metal-binding residues and β-sheet structural elements, highlighting their contribution to protein structure and function. Despite the capacity of ModA to bind chromate, deletion of did not affect PAO1 sensitivity to chromate toxicity nor impact cellular accumulation of chromate. Exposure to sub-inhibitory concentrations of chromate broadly perturbed metal homeostasis and, unexpectedly, was associated with an increase in ModA-mediated molybdenum uptake. Elemental analyses of the proteome from anaerobically grown revealed that, despite the increase in cellular molybdenum upon chromate exposure, distribution of the metal within the proteome was substantially perturbed. This suggested that molybdoprotein cofactor acquisition may be disrupted, consistent with the potent toxicity of chromate under anaerobic conditions. Collectively, these data reveal a complex relationship between chromate toxicity, molybdenum homeostasis and anaerobic respiration.

PubMed: 35685933
DOI: 10.3389/fmicb.2022.903146

Experimental method

X-RAY DIFFRACTION (1.9 Å)