Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip

Dunce J, Salmon L, Davies O, Communications Biology 5(1) (2022) DOI

SASDNP5 – Meiosis protein TEX12 (Testis-expressed protein 12) – delta Ctip

Testis-expressed protein 12
MWexperimental 29 kDa
MWexpected 32 kDa
VPorod 44 nm3
log I(s) 3.72×10-2 3.72×10-3 3.72×10-4 3.72×10-5
Testis-expressed protein 12 small angle scattering data  s, nm-1
ln I(s)
Testis-expressed protein 12 Guinier plot ln 3.73×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Testis-expressed protein 12 Kratky plot 1.104 0 √3 sRg
p(r)
Testis-expressed protein 12 pair distance distribution function Rg: 3.1 nm 0 Dmax: 11 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Testis-expressed protein 12 DAMMIF model
Testis-expressed protein 12 DAMFILT model
log I(s)
 s, nm-1
Testis-expressed protein 12 PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of the meiosis protein TEX12 (α-helical core, delta Ctip) in 20 mM Tris, 150 mM KCl, pH 8 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.095 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 32 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column. 20 successive 3 second frames were collected through the sample elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Testis-expressed protein 12 (TEX12 delta-Ctip)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   7.9 kDa
 
UniProt   Q9BXU0 (49-113)
Sequence   FASTA
 
PDB ID   6HK8