Structure of catabolite activator protein with cobalt(II) and sulfate
2014 ◽
Vol 70
(5)
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pp. 560-563
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Keyword(s):
The crystal structure of cyclic AMP–catabolite activator protein (CAP) fromEscherichia colicontaining 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 contributedviaa 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.
2004 ◽
Vol 14
(1)
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pp. 10-20
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Keyword(s):
1999 ◽
Vol 293
(2)
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pp. 199-213
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1992 ◽
Vol 267
(12)
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pp. 8136-8139
Keyword(s):
1995 ◽
Vol 177
(7)
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pp. 1712-1718
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1994 ◽
Vol 176
(17)
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pp. 5513-5524
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