Ontology highlight
ABSTRACT:
SUBMITTER: Lara-Gonzalez S
PROVIDER: S-EPMC2897699 | biostudies-literature | 2010 Jul
REPOSITORIES: biostudies-literature
Lara-González Samuel S Birktoft Jens J JJ Lawson Catherine L CL
Acta crystallographica. Section D, Biological crystallography 20100619 Pt 7
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) ...[more]