PDBsum entry 6yii

Signaling protein

PDB id: 6yii

Contents

Protein chain

473 a.a.

Ligands

ATP

SO4 ×3

Metals

_NA ×3

_MN

_CA

_MG

Waters ×642

PDB id:

6yii

Name:

Signaling protein

Title:

Crystal structure of a class iii adenylyl cyclase-like atp-binding protein from pseudomonas aeruginosa

Structure:

Transcriptional regulator. Chain: a. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Gene: caz10_26895, dz962_04370, ipc1509_03400, ipc170_13765, ipc669_21205. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Expression_system_variant: tuner prep groesl.

Resolution:

1.44Å R-factor: 0.131 R-free: 0.147

Authors:

S.Moniot,C.Steegborn

Key ref:

J.Linder et al. (2020). Crystal structure of a class III adenylyl cyclase-like ATP-binding protein from Pseudomonas aeruginosa. J Struct Biol, 211, 107534. PubMed id: 32454240 DOI: 10.1016/j.jsb.2020.107534

Date:

01-Apr-20 Release date: 17-Jun-20

Protein chain

P0DV40  (PYCC_PSEAI) -  Uridylate cyclase from Pseudomonas aeruginosa

Seq: 514 a.a.

Struc: 473 a.a.

Enzyme reactions

• Enzyme class: E.C.4.6.1.26 - uridylate cyclase.
• Reaction: UTP = 3',5'-cyclic UMP + diphosphate

UTP (Bound ligand (Het Group name = ATP) matches with 81.82% similarity) = 3',5'-cyclic UMP + diphosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.jsb.2020.107534

J Struct Biol 211:107534 (2020)

PubMed id: 32454240

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

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

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.