Structural highlights
Function
[Q9EZJ8_THEAQ] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (By similarity).[RuleBase:RU000715]
Publication Abstract from PubMed
Structural studies of -10 promoter element recognition by domain 2 of the RNA polymerase sigma subunit [Feklistov & Darst (2011), Cell, 147, 1257-1269] reveal an unusual crystal-packing arrangement dominated by G-quartets. The 3'-terminal GGG motif of the oligonucleotide used in crystallization participates in G-quadruplex formation with GGG motifs from symmetry-related complexes. Stacking between neighboring G-quadruplexes results in the formation of pseudo-continuous four-stranded columns running throughout the length of the crystal (G-columns). Here, a new crystal form is presented with a different arrangement of G-columns and it is proposed that the fortuitous finding of G-quartet packing could be useful in engineering crystal contacts in protein-ssDNA complexes.
Crystallographic analysis of an RNA polymerase sigma-subunit fragment complexed with -10 promoter element ssDNA: quadruplex formation as a possible tool for engineering crystal contacts in protein-ssDNA complexes.,Feklistov A, Darst SA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):950-5. doi:, 10.1107/S1744309113020368. Epub 2013 Aug 19. PMID:23989139[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feklistov A, Darst SA. Crystallographic analysis of an RNA polymerase sigma-subunit fragment complexed with -10 promoter element ssDNA: quadruplex formation as a possible tool for engineering crystal contacts in protein-ssDNA complexes. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):950-5. doi:, 10.1107/S1744309113020368. Epub 2013 Aug 19. PMID:23989139 doi:https://dx.doi.org/10.1107/S1744309113020368
