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Crystal structure of a class III adenylyl cyclase-like ATP-binding protein from Pseudomonas aeruginosa

Title data

Linder, Jürgen ; Hupfeld, Enrico ; Weyand, Michael ; Steegborn, Clemens ; Moniot, Sébastien:
Crystal structure of a class III adenylyl cyclase-like ATP-binding protein from Pseudomonas aeruginosa.
In: Journal of Structural Biology. Vol. 211 (August 2020) Issue 2 . - No. 107534.
ISSN 1047-8477
DOI: https://doi.org/10.1016/j.jsb.2020.107534

Abstract in another language

In many organisms, the ubiquitous second messenger cAMP is formed by at least one member of the adenylyl cyclase (AC) Class III. These ACs feature a conserved dimeric catalytic core architecture, either through homodimerization or through pseudo-heterodimerization of a tandem of two homologous catalytic domains, C1 and C2, on a single protein chain. The symmetric core features two active sites, but in the C1-C2 tandem one site degenerated into a regulatory center. Analyzing bacterial AC sequences, we identified a Pseudomonas aeruginosa AC-like protein (PaAClp) that shows a surprising swap of the catalytic domains, resulting in an unusual C2-C1 arrangement. We cloned and recombinantly produced PaAClp. The protein bound nucleotides but showed no AC or guanylyl cyclase activity, even in presence of a variety of stimulating ligands of other ACs. Solving the crystal structure of PaAClp revealed an overall structure resembling active class III ACs but pronounced shifts of essential catalytic residues and structural elements. The structure contains a tightly bound ATP, but in a binding mode not suitable for cAMP formation or ATP hydrolysis, suggesting that PaAClp acts as an ATP-binding protein.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: AC; ATP-binding; Anomalous scattering; Iodine; cAMP
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 07 Sep 2020 07:51
Last Modified: 07 Sep 2020 07:51
URI: https://eref.uni-bayreuth.de/id/eprint/56812