4v8s | pdb_00004v8s

Archaeal RNAP-DNA binary complex at 4.32Ang

spinqualitylabelsall models 4v8s, resolution 4.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v8s is a 30 chain structure with sequence from Sulfolobus shibatae b12. This structure supersedes the now removed PDB entries and 4b1p. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, SF4, ZN Related: 4b1o, 4b1p, 2y0s, 4ayb Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6 Resources: FirstGlance, OCA, RCSB, PDBsum Function [B8YB63_SULSH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00250] [B8YB61_SULSH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00192] [B8YB60_SULSH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00025] [B8YB54_SULSH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00411] [B8YB56_SULSH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00320] [B8YB64_SULSH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00615] [B8YB62_SULSH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00261] Publication Abstract from PubMed Multi-subunit RNA polymerases (RNAPs) in all three domains of life share a common ancestry. The composition of the archaeal RNAP (aRNAP) is not identical between phyla and species, with subunits Rpo8 and Rpo13 found in restricted subsets of archaea. While Rpo8 has an ortholog, Rpb8, in the nuclear eukaryal RNAPs, Rpo13 lacks clear eukaryal orthologs. Here, we report crystal structures of the DNA-bound and free form of the aRNAP from Sulfolobus shibatae. Together with biochemical and biophysical analyses, these data show that Rpo13 C-terminus binds non-specifically to double-stranded DNA. These interactions map on our RNAP-DNA binary complex on the downstream DNA at the far end of the DNA entry channel. Our findings thus support Rpo13 as a RNAP-DNA stabilization factor, a role reminiscent of eukaryotic general transcriptional factors. The data further yield insight into the mechanisms and evolution of RNAP-DNA interaction. Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA.,Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG Nucleic Acids Res. 2012 Jul 30. PMID:22848102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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