4g8x

G1 ORF67 / Staphyloccus aureus sigmaA domain 4 complex

spinqualitylabelsall models 4g8x, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g8x is a 4 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325 and Staphylococcus virus G1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.001Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SIGA_STAA8 Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Publication Abstract from PubMed Phage G1 gp67 is a 23 kDa protein that binds to the Staphylococcus aureus (Sau) RNA polymerase (RNAP) sigma(A) subunit and blocks cell growth by inhibiting transcription. We show that gp67 has little to no effect on transcription from most promoters but is a potent inhibitor of ribosomal RNA transcription. A 2.0-A-resolution crystal structure of the complex between gp67 and Sau sigma(A) domain 4 (sigma(A)(4)) explains how gp67 joins the RNAP promoter complex through sigma(A)(4) without significantly affecting sigma(A)(4) function. Our results indicate that gp67 forms a complex with RNAP at most, if not all, sigma(A)-dependent promoters, but selectively inhibits promoters that depend on an interaction between upstream DNA and the RNAP alpha-subunit C-terminal domain (alphaCTD). Thus, we reveal a promoter-specific transcription inhibition mechanism by which gp67 interacts with the RNAP promoter complex through one subunit (sigma(A)), and selectively affects the function of another subunit (alphaCTD) depending on promoter usage. Promoter-specific transcription inhibition in Staphylococcus aureus by a phage protein.,Osmundson J, Montero-Diez C, Westblade LF, Hochschild A, Darst SA Cell. 2012 Nov 21;151(5):1005-16. doi: 10.1016/j.cell.2012.10.034. PMID:23178120 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sigma factor 3D structures

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