6YII

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

Summary for 6YII

• Entry DOI: 10.2210/pdb6yii/pdb
• Descriptor: Transcriptional regulator, ADENOSINE-5'-TRIPHOSPHATE, MANGANESE (II) ION, ... (8 entities in total)
• Functional Keywords: atp complex, class iii adenylyl cyclase fold, signaling protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 57645.99

Authors

Moniot, S.,Steegborn, C. (deposition date: 2020-04-01, release date: 2020-06-17, Last modification date: 2024-05-15)

Primary citation

Linder, J.,Hupfeld, E.,Weyand, M.,Steegborn, C.,Moniot, S.
Crystal structure of a class III adenylyl cyclase-like ATP-binding protein from Pseudomonas aeruginosa.
J.Struct.Biol., 211:107534-107534, 2020

PubMed Abstract: 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.

PubMed: 32454240
DOI: 10.1016/j.jsb.2020.107534

Experimental method

X-RAY DIFFRACTION (1.44 Å)