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Article

The 1.6Å resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer.

International journal of biological macromolecules - 1 Apr 2011

Tao Wenbing, Gao Zengqiang, Gao Zhengya, Zhou Jiahai, Huang Zhongxian, Dong Yuhui, Yu Shaoning

Abstract excerpt

The X-ray crystal structure of the cAMP-liganded D138L mutant of Escherichia coli catabolite gene activator protein (CAP) was determined at a resolution of 1.66Å. This high resolution crystal structure reveals four cAMP binding sites in the homodimer. Two anti conformations of cAMPs (anti-cAMP) locate between the β-barrel and the C-helix of each subunit; two syn conformations of cAMPs (syn-cAMP) bind on the...

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PMID: 21255606
DOI: 10.1016/j.ijbiomac.2011.01.009

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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