Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery

Nasta V, Da Vela S, Gourdoupis S, Ciofi-Baffoni S, Svergun D, Banci L, Scientific Reports 9(1) (2019) DOI

SASDGD2 – Putative mitochondrial transferase CAF17: human IBA57

Putative transferase CAF17, mitochondrial
MWexperimental 26 kDa
MWexpected 33 kDa
VPorod 50 nm3
log I(s) 1.77×102 1.77×101 1.77×100 1.77×10-1
Putative transferase CAF17, mitochondrial small angle scattering data  s, nm-1
ln I(s)
Putative transferase CAF17, mitochondrial Guinier plot ln 1.77×102 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Putative transferase CAF17, mitochondrial Kratky plot 1.104 0 √3 sRg
p(r)
Putative transferase CAF17, mitochondrial pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Putative transferase CAF17, mitochondrial PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of human IBA57 in 50 mM phosphate, 150 mM NaCl, 5 mM DTT, pH 7 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 100.00 μl sample at 5 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 3000 successive 0.995 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.

Putative transferase CAF17, mitochondrial (IBA57)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   33.2 kDa
 
UniProt   Q5T440 (44-352)
Sequence   FASTA
 
PDB ID   6QE3