5YIU
Caulobacter crescentus GcrA DNA-binding domain (DBD)
Summary for 5YIU
| Entry DOI | 10.2210/pdb5yiu/pdb |
| Descriptor | Cell cycle regulatory protein GcrA (2 entities in total) |
| Functional Keywords | caulobacter crescentus, gcra, dna-binding, transcription factor, dna binding protein |
| Biological source | Caulobacter crescentus (strain NA1000 / CB15N) |
| Total number of polymer chains | 1 |
| Total formula weight | 5317.20 |
| Authors | |
| Primary citation | Wu, X.,Haakonsen, D.L.,Sanderlin, A.G.,Liu, Y.J.,Shen, L.,Zhuang, N.,Laub, M.T.,Zhang, Y. Structural insights into the unique mechanism of transcription activation by Caulobacter crescentus GcrA. Nucleic Acids Res., 46:3245-3256, 2018 Cited by PubMed Abstract: Canonical bacterial transcription activators bind to non-transcribed promoter elements to increase transcription of their target genes. Here we report crystal structures of binary complexes comprising domains of Caulobacter crescentus GcrA, a noncanonical bacterial transcription factor, that support a novel mechanism for transcription activation through the preferential binding of methylated cis-regulatory elements and the promotion of open complex formation through an interaction with region 2 of the principal σ factor, σ70. We present crystal structures of the C-terminal, σ factor-interacting domain (GcrA-SID) in complex with domain 2 of σ70 (σ702), and the N-terminal, DNA-binding domain (GcrA-DBD) in complex with methylated double-stranded DNA (dsDNA). The structures reveal interactions essential for transcription activation and DNA recognition by GcrA. These structures, along with mutational analyses, support a mechanism of transcription activation in which GcrA associates with RNA polymerase (RNAP) prior to promoter binding through GcrA-SID, arming RNAP with a flexible GcrA-DBD. The RNAP-GcrA complex then binds and activates target promoters harboring a methylated GcrA binding site either upstream or downstream of the transcription start site. PubMed: 29514271DOI: 10.1093/nar/gky161 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.42 Å) |
Structure validation
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