8X6G
Cryo-EM structure of Staphylococcus aureus sigB-dependent RNAP-promoter open complex
Summary for 8X6G
Entry DOI | 10.2210/pdb8x6g/pdb |
EMDB information | 38088 |
Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total) |
Functional Keywords | rna polymerase, transcription, staphylococcus aureus, sigb |
Biological source | Staphylococcus aureus More |
Total number of polymer chains | 10 |
Total formula weight | 449506.20 |
Authors | |
Primary citation | Yuan, L.,Liu, Q.,Xu, L.,Wu, B.,Feng, Y. Structural basis of promoter recognition by Staphylococcus aureus RNA polymerase. Nat Commun, 15:4850-4850, 2024 Cited by PubMed Abstract: Bacterial RNAP needs to form holoenzyme with σ factors to initiate transcription. While Staphylococcus aureus σ controls housekeeping functions, S. aureus σ regulates virulence, biofilm formation, persistence, cell internalization, membrane transport, and antimicrobial resistance. Besides the sequence difference, the spacers between the -35 element and -10 element of σ regulated promoters are shorter than those of σ regulated promoters. Therefore, how σ recognizes and initiates transcription from target promoters can not be inferred from that of the well studied σ. Here, we report the cryo-EM structures of S. aureus RNAP-promoter open complexes comprising σ and σ, respectively. Structural analyses, in combination with biochemical experiments, reveal the structural basis for the promoter specificity of S. aureus transcription. Although the -10 element of σ regulated promoters is recognized by domain σ as single-stranded DNA, the -10 element of σ regulated promoters is co-recognized by domains σ and σ as double-stranded DNA, accounting for the short spacers of σ regulated promoters. S. aureus RNAP is a validated target of antibiotics, and our structures pave the way for rational drug design targeting S. aureus RNAP. PubMed: 38844782DOI: 10.1038/s41467-024-49229-6 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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