Biotin repressor stress
WebMay 15, 1998 · The Escherichia coli repressor of biotin biosynthesis, BirA, binds to a 40 bp operator site (bioO) to repress transcriptional initiation at the two divergent promoters of the biotin biosynthetic operon (Figure 1A; Otsuka & Abelson, 1978). WebDec 25, 1982 · A bifunctional protein. Definitive evidence is presented for the bifunctional …
Biotin repressor stress
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WebOct 1, 1992 · The three-dimensional structure of BirA, the repressor of the Escherichia … WebSep 24, 1999 · The Escherichia coli repressor of biotin biosynthesis (BirA) is an allosteric site-specific DNA-binding protein. BirA catalyzes synthesis of biotinyl-5′-AMP from substrates biotin and ATP and the adenylate serves as the positive allosteric effector in binding of the repressor to the biotin operator sequence.
WebJan 12, 2001 · The Escherichia coli biotin repressor binds to the biotin operator to repress transcription of the biotin biosynthetic operon. In this work, a structure determined by x-ray crystallography of a complex of the repressor bound to biotin, which also functions as an activator of DNA binding by the biotin repressor (BirA), is described ... WebSep 11, 2014 · Small ligand, bio-5'-AMP, binding and dimerization of the Escherichia coli biotin repressor are allosterically coupled ... Macromolecules Find similar proteins by: (by identity cutoff) 3D Structure Small Molecules Experimental Data & Validation Experimental Data Method: X-RAY DIFFRACTION Resolution: 2.31 Å R-Value Free: 0.218 R-Value …
WebJan 1, 2001 · Cooperative association of the Escherichia coli biotin repressor with the biotin operator is allosterically activated by binding of the corepressor, bio-5'-AMP. The corepressor function of...
WebFeb 1, 2003 · The biotin repressor is an allosterically regulated, site-specific DNA-binding protein. Binding of the small ligand bio-5'-AMP activates repressor dimerization, which is a prerequisite to DNA binding.
WebAug 1, 2008 · The biotin repressor is an allosterically regulated, site-specific DNA-binding protein. Binding of the small ligand bio-5′-AMP activates repressor dimerization, which is a prerequisite to DNA binding.Multiple disorder-to-order transitions, some of which are known to be important for the functional allosteric response, occur in the vicinity of the ligand … grace kelly gownsWebNov 14, 2024 · Acid stress reduces the internal pH below this threshold, increasing OmpR dimerization and DNA binding. ... in the ompR null mutant, suggesting that E. coli OmpR also functions as a repressor at ... grace kelly gundermanWebFeb 13, 1996 · The Escherichia coli repressor of biotin biosynthesis (BirA) is an allosteric site-specific DNA binding protein. The protein is composed of three structural domains. Contact with the biotin operator (bioO) in the transcriptional repression complex is made by the N-terminal domain which contains a helix−turn−helix structural module. The … chillicothe topixWebNov 4, 2005 · The co-repressor buttresses the dimer interface, resulting in improved packing and a 12 degrees change in the hinge-bending angle along the dimer interface relative to the BirA.biotin structure. This helps explain why the binding of the co-repressor is necessary to optimize the binding of BirA to the bioO operator. chillicothe tire discountersWebEnzymatic Biotinylation: BirA. Ligation of biotin to a protein is a specific post-translational … grace kelly grandchildren picsWebFeb 2, 2005 · The Escherichia coli biotin repressor is an allosteric DNA binding protein and is activated by the small molecule bio-5‘-AMP. Binding of this small molecule promotes transcription repression complex assembly between the repressor and the biotin operator of the biotin biosynthetic operon. chillicothe title deptWebConsist- ent with the presence of the biotin repressor BirA, ... Genomic organization of genes involved in oxidative stress response Figure 9 Genomic organization of genes involved in oxidative ... chillicothe to columbus