view article

Figure 3
Domain structure comparisons. (a) Superimposition of the DUF2063 domain (residues 31–116) of NGO1945 (gray) with the σ2 domain of RNA polymerase sigma factor SigR from S. coelicolor (PDB code 1h3l , cyan), the SAM domain of the transcription elongation factor NusA (1u9l , yellow) and the N-terminal domain of STE50 (1uqv , red). (b) Superimposition of NGO1945 residues 117–174 (gray) with the WW domain of human FE65 (2idh , pink), monellin (3mon , red) and the N-terminal domain of the ribosomal protein L11 from T. maritima (1mms , yellow). (c) Comparison of NGO1945 residues 175–231 (gray) with the Z-DNA-binding domain of the vaccinia virus E3L protein (1oyi , green), the DNA-binding domain of MafG bZIP (1k1v , blue) and the Nanog homeodomain (2vi6 , orange). (d) Superimposition of NGO1945 residues 117–231 (gray) with the transcription repressor MecI (1okr , green) and the DNA-binding domain of the response regulator PhoP (2pmu , pink).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds