7Z06
Structure of YwlG (Q2FF14) from Staphylococcus aureus
7Z06 の概要
エントリーDOI | 10.2210/pdb7z06/pdb |
分子名称 | UPF0340 protein SAUSA300_2068, SULFATE ION (3 entities in total) |
機能のキーワード | hexameric complex, unknown function |
由来する生物種 | Staphylococcus aureus |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 129689.18 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 36122228DOI: 10.1073/pnas.2207257119 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.74 Å) |
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