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

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.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Linder J,Hupfeld E,Weyand M,Steegborn C,Moniot S

doi

10.1016/j.jsb.2020.107534

subject

Has Abstract

pub_date

2020-08-01 00:00:00

pages

107534

issue

2

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(20)30107-6

journal_volume

211

pub_type

杂志文章

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