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Structure of catabolite activator protein with cobalt(II) and sulfate

The crystal structure of cyclic AMP–catabolite activator protein (CAP) from Escherichia coli containing cobalt(II) chloride and ammonium sulfate is reported at 1.97 Å resolution. Each of the two CAP subunits in the asymmetric unit binds one cobalt(II) ion, in each case coordinated by N-terminal doma...

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Autores principales: Rao, Ramya R., Lawson, Catherine L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4014319/
https://www.ncbi.nlm.nih.gov/pubmed/24817710
http://dx.doi.org/10.1107/S2053230X14005366
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author Rao, Ramya R.
Lawson, Catherine L.
author_facet Rao, Ramya R.
Lawson, Catherine L.
author_sort Rao, Ramya R.
collection PubMed
description The crystal structure of cyclic AMP–catabolite activator protein (CAP) from Escherichia coli containing cobalt(II) chloride and ammonium sulfate is reported at 1.97 Å resolution. Each of the two CAP subunits in the asymmetric unit binds one cobalt(II) ion, in each case coordinated by N-terminal domain residues His19, His21 and Glu96 plus an additional acidic residue contributed via a crystal contact. The three identified N-terminal domain cobalt-binding residues are part of a region of CAP that is important for transcription activation at class II CAP-dependent promoters. Sulfate anions mediate additional crystal lattice contacts and occupy sites corresponding to DNA backbone phosphate positions in CAP–DNA complex structures.
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spelling pubmed-40143192014-06-05 Structure of catabolite activator protein with cobalt(II) and sulfate Rao, Ramya R. Lawson, Catherine L. Acta Crystallogr F Struct Biol Commun Structural Communications The crystal structure of cyclic AMP–catabolite activator protein (CAP) from Escherichia coli containing cobalt(II) chloride and ammonium sulfate is reported at 1.97 Å resolution. Each of the two CAP subunits in the asymmetric unit binds one cobalt(II) ion, in each case coordinated by N-terminal domain residues His19, His21 and Glu96 plus an additional acidic residue contributed via a crystal contact. The three identified N-terminal domain cobalt-binding residues are part of a region of CAP that is important for transcription activation at class II CAP-dependent promoters. Sulfate anions mediate additional crystal lattice contacts and occupy sites corresponding to DNA backbone phosphate positions in CAP–DNA complex structures. International Union of Crystallography 2014-04-15 /pmc/articles/PMC4014319/ /pubmed/24817710 http://dx.doi.org/10.1107/S2053230X14005366 Text en © Rao & Lawson 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Structural Communications
Rao, Ramya R.
Lawson, Catherine L.
Structure of catabolite activator protein with cobalt(II) and sulfate
title Structure of catabolite activator protein with cobalt(II) and sulfate
title_full Structure of catabolite activator protein with cobalt(II) and sulfate
title_fullStr Structure of catabolite activator protein with cobalt(II) and sulfate
title_full_unstemmed Structure of catabolite activator protein with cobalt(II) and sulfate
title_short Structure of catabolite activator protein with cobalt(II) and sulfate
title_sort structure of catabolite activator protein with cobalt(ii) and sulfate
topic Structural Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4014319/
https://www.ncbi.nlm.nih.gov/pubmed/24817710
http://dx.doi.org/10.1107/S2053230X14005366
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