7Z06

Structure of YwlG (Q2FF14) from Staphylococcus aureus

Summary for 7Z06

• Entry DOI: 10.2210/pdb7z06/pdb
• Descriptor: UPF0340 protein SAUSA300_2068, SULFATE ION (3 entities in total)
• Functional Keywords: hexameric complex, unknown function
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 6
• Total formula weight: 129689.18

Authors

Schneider, S.,Scheidler, C.M.,Sieber, S.A. (deposition date: 2022-02-22, release date: 2022-09-21, Last modification date: 2024-01-31)

Primary citation

Ranava, D.,Scheidler, C.M.,Pfanzelt, M.,Fiedler, M.,Sieber, S.A.,Schneider, S.,Yap, M.F.
Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.
Proc.Natl.Acad.Sci.USA, 119:e2207257119-e2207257119, 2022

PubMed Abstract: Bacterial hibernating 100S ribosomes (the 70S dimers) are excluded from translation and are protected from ribonucleolytic degradation, thereby promoting long-term viability and increased regrowth. No extraribosomal target of any hibernation factor has been reported. Here, we discovered a previously unrecognized binding partner (YwlG) of hibernation-promoting factor (HPF) in the human pathogen . YwlG is an uncharacterized virulence factor in . We show that the HPF-YwlG interaction is direct, independent of ribosome binding, and functionally linked to cold adaptation and glucose metabolism. Consistent with the distant resemblance of YwlG to the hexameric structures of nicotinamide adenine dinucleotide (NAD)-specific glutamate dehydrogenases (GDHs), YwlG overexpression can compensate for a loss of cellular GDH activity. The reduced abundance of 100S complexes and the suppression of YwlG-dependent GDH activity provide evidence for a two-way sequestration between YwlG and HPF. These findings reveal an unexpected layer of regulation linking the biogenesis of 100S ribosomes to glutamate metabolism.

PubMed: 36122228
DOI: 10.1073/pnas.2207257119

Experimental method

X-RAY DIFFRACTION (1.74 Å)