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5EZF

Racemic crystal structures of Pribnow box consensus promoter sequence (Pbca)

Summary for 5EZF
Entry DOI10.2210/pdb5ezf/pdb
Related5ET9 5EWB 5EYQ
DescriptorPribnow box template strand, Complementary strand, CALCIUM ION, ... (4 entities in total)
Functional Keywordspribnow box consensus sequence, -10 element, transcription initiation, b-dna double helix, dna double helix, dna
Biological sourcesynthetic construct
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Total number of polymer chains2
Total formula weight7404.96
Authors
Mandal, P.K.,Collie, G.W.,Kauffmann, B.,Srivastava, S.C.,Huc, I. (deposition date: 2015-11-26, release date: 2016-05-18, Last modification date: 2024-01-10)
Primary citationMandal, P.K.,Collie, G.W.,Srivastava, S.C.,Kauffmann, B.,Huc, I.
Structure elucidation of the Pribnow box consensus promoter sequence by racemic DNA crystallography.
Nucleic Acids Res., 44:5936-5943, 2016
Cited by
PubMed Abstract: It has previously been shown that the use of racemic mixtures of naturally chiral macromolecules such as protein and DNA can significantly aid the crystallogenesis process, thereby addressing one of the major bottlenecks to structure determination by X-ray crystallographic methods-that of crystal growth. Although previous studies have provided convincing evidence of the applicability of the racemic crystallization technique to DNA through the study of well-characterized DNA structures, we sought to apply this method to a historically challenging DNA sequence. For this purpose we chose a non-self-complementary DNA duplex containing the biologically-relevant Pribnow box consensus sequence 'TATAAT'. Four racemic crystal structures of this previously un-crystallizable DNA target are reported (with resolutions in the range of 1.65-2.3 Å), with further crystallographic studies and structural analysis providing insight into the racemic crystallization process as well as structural details of this highly pertinent DNA sequence.
PubMed: 27137886
DOI: 10.1093/nar/gkw367
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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数据于2025-06-18公开中

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