4NJC
RNA Polymerase interacting protein YkzG from Geobacillus stearothermophilus
Summary for 4NJC
| Entry DOI | 10.2210/pdb4njc/pdb |
| Descriptor | Geobacillus stearothermophilus YkzG (2 entities in total) |
| Functional Keywords | dna dependant rna polymerase, transcription |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 8 |
| Total formula weight | 64692.95 |
| Authors | Keller, A.N.,Lewis, P.J. (deposition date: 2013-11-09, release date: 2014-08-20, Last modification date: 2024-11-13) |
| Primary citation | Keller, A.N.,Yang, X.,Wiedermannova, J.,Delumeau, O.,Krasny, L.,Lewis, P.J. epsilon, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria J.Bacteriol., 196:3622-3632, 2014 Cited by PubMed Abstract: RNA polymerase in bacteria is a multisubunit protein complex that is essential for gene expression. We have identified a new subunit of RNA polymerase present in the high-A+T Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω1) that copurified with RNA polymerase. We have solved the structure of ε by X-ray crystallography and show that it is not an ω subunit. Rather, ε bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of ε shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of ε within the assembly of RNA polymerase core by single-particle analysis suggests that it binds toward the downstream side of the DNA binding cleft. Due to the structural similarity of ε with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that ε may serve a role in protection from phage infection. PubMed: 25092033DOI: 10.1128/JB.02020-14 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report






