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

The crystal structure of E. coli catabolite activator protein with bound cobalt(II) and sulfate ions at 1.97 Å resolution is reported. 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.
Authors:
;  [1]
  1. Rutgers University, Piscataway, NJ 08854 (United States)
Publication Date:
OSTI Identifier:
22375686
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta crystallographica. Section F, Structural biology communications; Journal Volume: 70; Journal Issue: Pt 5; Other Information: PMCID: PMC4014319; PMID: 24817710; PUBLISHER-ID: fw5447; OAI: oai:pubmedcentral.nih.gov:4014319; Copyright (c) Rao & Lawson 2014; 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.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AMMONIUM SULFATES; ANIONS; COBALT; CRYSTAL LATTICES; CRYSTALS; DNA; ESCHERICHIA COLI; PHOSPHATES; PROTEINS; RESOLUTION