7v5z | pdb_00007v5z

Crystal structure of heterotetrameric complex of Sa2YoeB-Sa2YefM toxin-antitoxin from Staphylococcus aureus

spinqualitylabelsall models 7v5z, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7v5z is a 4 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.99Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2FVF7_STAA8 Antitoxin component of a type II toxin-antitoxin (TA) system.[RuleBase:RU362080] Publication Abstract from PubMed Toxin-antitoxin (TA) systems are ubiquitous regulatory modules for bacterial growth and cell survival following stress. YefM-YoeB, the most prevalent type II TA system, is present in a variety of bacterial species. In Staphylococcus aureus, the YefM-YoeB system exists as two independent paralogous copies. Our previous research resolved crystal structures of the two oligomeric states (heterotetramer and heterohexamer-DNA ternary complex) of the first paralog as well as the molecular mechanism of transcriptional autoregulation of this module. However, structural details reflecting molecular diversity in both paralogs have been relatively unexplored. To understand the molecular mechanism of how Sa(2)YoeB and Sa(2)YefM regulate their own transcription and how each paralog functions independently, we solved a series of crystal structures of the Sa(2)YoeB-Sa(2)YefM. Our structural and biochemical data demonstrated that both paralogous copies adopt similar mechanisms of transcriptional autoregulation. In addition, structural analysis suggested that molecular diversity between the two paralogs might be reflected in the interaction profile of YefM and YoeB and the recognition pattern of promoter DNA by YefM. Interaction analysis revealed unique conformational and activating force effected by the interface between Sa(2)YoeB and Sa(2)YefM. In addition, the recognition pattern analysis demonstrated that residues Thr(7) and Tyr(14) of Sa(2)YefM specifically recognizes the flanking sequences (G and C) of the promoter DNA. Together, these results provide the structural insights into the molecular diversity and independent function of the paralogous copies of the YoeB-YefM TA system. The two paralogous copies of the YoeB-YefM toxin-antitoxin module in Staphylococcus aureus differ in DNA binding and recognition patterns.,Xue L, Khan MH, Yue J, Zhu Z, Niu L J Biol Chem. 2022 Jan;298(1):101457. doi: 10.1016/j.jbc.2021.101457. Epub 2021 , Nov 30. PMID:34861238 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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