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Structure of the Escherichia coli RNA polymerase α subunit C-terminal domain

✍ Scribed by Lara-González, Samuel ;Birktoft, Jens J. ;Lawson, Catherine L.

Publisher
International Union of Crystallography
Year
2010
Tongue
English
Weight
883 KB
Volume
66
Category
Article
ISSN
0907-4449

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✦ Synopsis

The α subunit C-terminal domain (αCTD) 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__αCTD (α subunit residues 245–329) determined to 2.0 Å resolution is reported. Crystals were obtained after reductive methylation of the recombinantly expressed domain. The crystals belonged to space group__P__2~1~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 αCTD 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 αCTD-containing multi-component complexes visualized at lower resolution using X-ray crystallography and electron-microscopy reconstruction.

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