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5Z7I

Caulobacter crescentus GcrA DNA-binding domain(DBD)in complex with unmethylated dsDNA

Summary for 5Z7I
Entry DOI10.2210/pdb5z7i/pdb
DescriptorCell cycle regulatory protein GcrA, DNA (5'-D(*CP*CP*CP*TP*GP*AP*TP*TP*CP*GP*C*)-3'), DNA (5'-D(P*GP*CP*GP*AP*AP*TP*CP*AP*GP*G)-3'), ... (5 entities in total)
Functional Keywordscaulobacter crescentus, gcra, dna-binding, transcription factor, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
Biological sourceCaulobacter crescentus (strain NA1000 / CB15N)
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Total number of polymer chains5
Total formula weight22420.91
Authors
Wu, X.,Zhang, Y. (deposition date: 2018-01-29, release date: 2018-03-21, Last modification date: 2024-04-03)
Primary citationWu, 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: 29514271
DOI: 10.1093/nar/gky161
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.601 Å)
Structure validation

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