ISDA: 1BDF

Deposition Date 1998-05-08

Release Date 1999-05-11

Last Version Date 2024-02-07

Entry Detail

PDB ID:

1BDF

Keywords:

NUCLEOTIDYLTRANSFERASE

Title:

STRUCTURE OF ESCHERICHIA COLI RNA POLYMERASE ALPHA SUBUNIT N-TERMINAL DOMAIN

Biological Source:

Source Organism(s):

Escherichia coli (Taxon ID: 562)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.50 Å

R-Value Free:

0.30

R-Value Work:

0.22

R-Value Observed:

0.22

Space Group:

H 3 2

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:RNA POLYMERASE ALPHA SUBUNIT
Gene (Uniprot):rpoA
Mutagens:R45A
Chain IDs:A, B, C, D
Chain Length:235
Number of Molecules:4
Biological Source:Escherichia coli

UniProt ID:P0A7Z4 Pfam ID:PF01193, PF01000 EC:2.7.7.6

Primary Citation

Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain.

Zhang, G, Darst, S.A.Show

Science 281 262 266 (1998)

PMID: 9657722 DOI: 10.1126/science.281.5374.262

Abstact

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.

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Primary Citation of related structures

Abstact

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