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Nucleotide binding by the histidine kinase CheA

Autor: A M, Bilwes, C M, Quezada, L R, Croal, B R, Crane, M I, Simon

Publikováno v: Nature structural biology. 8(4)

To probe the structural basis for protein histidine kinase (PHK) catalytic activity and the prospects for PHK-specific inhibitor design, we report the crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::44d49bc50652a30ecf62d7e19f21f60c
https://pubmed.ncbi.nlm.nih.gov/11276258

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The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR

Autor: L J, Donald, B R, Crane, D H, Anderson, H W, Duckworth

Publikováno v: The Journal of biological chemistry. 266(31)

Escherichia coli citrate synthase is strongly and specifically inhibited by NADH, but this inhibition can be prevented by reacting the enzyme with Ellman's reagent. We have now labeled the single reactive cysteine covalently with monobromobimane and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::72ba48c6f32c0ef6574751373e537781
https://pubmed.ncbi.nlm.nih.gov/1939121

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Improved phases, phase error estimates and anomalous scattering models from the multiwavelength anomalous diffraction (MAD) of native protein metal clusters

Autor: E. D. Getzoff, B. R. Crane

Publikováno v: Acta Crystallographica Section A Foundations of Crystallography. 52:C57-C58

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0004e5993d9193f91de374fe9665fca5
https://doi.org/10.1107/s0108767396096717

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