3K4G
Crystal structure of E. coli RNA polymerase alpha subunit C-terminal domain
Summary for 3K4G
| Entry DOI | 10.2210/pdb3k4g/pdb |
| Descriptor | DNA-directed RNA polymerase subunit alpha, SODIUM ION (3 entities in total) |
| Functional Keywords | bacterial transcription regulation, dna-directed rna polymerase, nucleotidyltransferase, transcription, transferase |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 8 |
| Total formula weight | 78391.02 |
| Authors | Lara-Gonzalez, S.,Birktoft, J.,Lawson, C.L. (deposition date: 2009-10-05, release date: 2010-07-07, Last modification date: 2023-09-06) |
| Primary citation | Lara-Gonzalez, S.,Birktoft, J.J.,Lawson, C.L. Structure of the Escherichia coli RNA polymerase alpha subunit C-terminal domain. Acta Crystallogr.,Sect.D, 66:806-812, 2010 Cited by PubMed Abstract: The alpha subunit C-terminal domain (alphaCTD) of RNA polymerase (RNAP) is a key element in transcription activation in Escherichia coli, possessing determinants responsible for the interaction of RNAP with DNA and with transcription factors. Here, the crystal structure of E. coli alphaCTD (alpha subunit residues 245-329) determined to 2.0 A resolution is reported. Crystals were obtained after reductive methylation of the recombinantly expressed domain. The crystals belonged to space group P2(1) and possessed both pseudo-translational symmetry and pseudo-merohedral twinning. The refined coordinate model (R factor = 0.193, R(free) = 0.236) has improved geometry compared with prior lower resolution determinations of the alphaCTD structure [Jeon et al. (1995), Science, 270, 1495-1497; Benoff et al. (2002), Science, 297, 1562-1566]. An extensive dimerization interface formed primarily by N- and C-terminal residues is also observed. The new coordinates will facilitate the improved modeling of alphaCTD-containing multi-component complexes visualized at lower resolution using X-ray crystallography and electron-microscopy reconstruction. PubMed: 20606261DOI: 10.1107/S0907444910018470 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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