Mechanistic and structural insights into the bifunctional enzyme PaaY from Acinetobacter baumannii.

Jiao M, He W, Ouyang Z, Qin Q, Guo Y, Zhang J, Bai Y, Guo X, Yu Q, She J, Hwang PM, Zheng F, Wen Y, Structure (2023) Europe PMC

SASDP69 – Acinetobacter baumannii carbonic anhydrase PaaY trimer

Bacterial transferase hexapeptide repeat protein
MWexperimental 71 kDa
MWexpected 66 kDa
VPorod 102 nm3
log I(s) 5.54×101 5.54×100 5.54×10-1 5.54×10-2
Bacterial transferase hexapeptide repeat protein small angle scattering data  s, nm-1
ln I(s)
Bacterial transferase hexapeptide repeat protein Guinier plot ln 5.54×101 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Bacterial transferase hexapeptide repeat protein Kratky plot 1.104 0 √3 sRg
Dmax: 9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Bacterial transferase hexapeptide repeat protein CORAL model
Synchrotron SAXS data from solutions of Acinetobacter baumannii carbonic anhydrase PaaY trimer in 20 mM Tris, 150 mM NaCl, pH 7.4 were collected on the BL19U2 beam line at the Shanghai Synchrotron Radiation Facility (SSRF; Shanghai, China) using a Pilatus 1M detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.00 mg/ml was measured at 23°C. 20 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Bacterial transferase hexapeptide repeat protein
Mol. type   Protein
Organism   Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81)
Olig. state   Trimer
Mon. MW   21.9 kDa
 
UniProt   D0C8J4 (1-201)
Sequence   FASTA