A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria.

Grosjean N, Yee EF, Kumaran D, Chopra K, Abernathy M, Biswas S, Byrnes J, Kreitler DF, Cheng JF, Ghosh A, Almo SC, Iwai M, Niyogi KK, Pakrasi HB, Sarangi R, van Dam H, Yang L, Blaby IK, Blaby-Haas CE, Nat Commun 15(1):3167 (2024) Europe PMC

SASDRG5 – A ssr1698 Dri1 hemoprotein, wild-type (apo) variant + heme

Ssr1698 protein
MWexperimental 24 kDa
MWexpected 23 kDa
VPorod 29 nm3
log I(s) 9.33×100 9.33×10-1 9.33×10-2 9.33×10-3
Ssr1698 protein small angle scattering data  s, nm-1
ln I(s)
Ssr1698 protein Guinier plot ln 9.33×100 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Ssr1698 protein Kratky plot 1.104 0 √3 sRg
p(r)
Ssr1698 protein pair distance distribution function Rg: 2.0 nm 0 Dmax: 6.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Synchrotron SAXS data from solutions of a ssr1698 Dri1 hemoprotein, wild-type (apo) variant + heme in 50 mM Hepes, 200 mM NaCl, pH 7.5 were collected on the 16-ID (LiX) beam line at the National Synchrotron Light Source II (NSLS-II, Upton, NY, USA) using Pilatus3 X 1M and Pilatus3 X 900K duel detectors at sample-detector distances of 3.76 and 0.343 m, respectively, and at a wavelength of λ = 0.08188 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 90.00 μl sample was injected at a 0.50 ml/min flow rate onto a Biozen 3 µm dSEC-2, 200 Å column at 4°C. 13 successive 2 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.

Ssr1698 protein
Mol. type   Protein
Organism   Synechocystis sp. (strain PCC 6803 / Kazusa)
Olig. state   Dimer
Mon. MW   11.3 kDa
 
UniProt   P73129 (1-96)
Sequence   FASTA