1bdf
From Proteopedia
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STRUCTURE OF ESCHERICHIA COLI RNA POLYMERASE ALPHA SUBUNIT N-TERMINAL DOMAIN
Overview
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.
About this Structure
1BDF is a Single protein structure of sequence from Escherichia coli. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain., Zhang G, Darst SA, Science. 1998 Jul 10;281(5374):262-6. PMID:9657722
Page seeded by OCA on Tue Nov 20 11:33:52 2007
