1BDF
STRUCTURE OF ESCHERICHIA COLI RNA POLYMERASE ALPHA SUBUNIT N-TERMINAL DOMAIN
Summary for 1BDF
| Entry DOI | 10.2210/pdb1bdf/pdb |
| Descriptor | RNA POLYMERASE ALPHA SUBUNIT (2 entities in total) |
| Functional Keywords | nucleotidyltransferase, rnap, alpha, assemble |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 103653.97 |
| Authors | Zhang, G.,Darst, S.A. (deposition date: 1998-05-08, release date: 1999-05-11, Last modification date: 2024-02-07) |
| Primary citation | Zhang, G.,Darst, S.A. Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain. Science, 281:262-266, 1998 Cited by PubMed Abstract: The 2.5 angstrom resolution x-ray crystal structure of the Escherichia coli RNA polymerase (RNAP) alpha subunit amino-terminal domain (alphaNTD), which is necessary and sufficient to dimerize and assemble the other RNAP subunits into a transcriptionally active enzyme and contains all of the sequence elements conserved among eukaryotic alpha homologs, has been determined. The alphaNTD monomer comprises two distinct, flexibly linked domains, only one of which participates in the dimer interface. In the alphaNTD dimer, a pair of helices from one monomer interact with the cognate helices of the other to form an extensive hydrophobic core. All of the determinants for interactions with the other RNAP subunits lie on one face of the alphaNTD dimer. Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to Saccharomyces cerevisiae Rpb3 and Rpb11 plays the role of the alphaNTD dimer in prokaryotic RNAP. PubMed: 9657722DOI: 10.1126/science.281.5374.262 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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