Evidence of Reciprocal Reorientation of the Catalytic and Hemopexin-Like Domains of Full-Length MMP-12

Bertini I, Calderone V, Fragai M, Jaiswal R, Luchinat C, Melikian M, Mylonas E, Svergun D, Journal of the American Chemical Society 130(22):7011-7021 (2008) DOI

SASDNC2 – NNGH-inhibited, cadmium(II)-substituted Phe171Asp/Glu219Ala double mutant of FL-MMP- 12

Macrophage metalloelastase
MWexperimental 40 kDa
MWexpected 54 kDa
VPorod 58 nm3
log I(s) 1.61×102 1.61×101 1.61×100 1.61×10-1
Macrophage metalloelastase small angle scattering data  s, nm-1
ln I(s)
Macrophage metalloelastase Guinier plot ln 1.62×102 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Macrophage metalloelastase Kratky plot 1.104 0 √3 sRg
p(r)
Macrophage metalloelastase pair distance distribution function Rg: 3.2 nm 0 Dmax: 11 nm

Data validation

Fits and models

log I(s)
 s, nm-1
NNGH-inhibited, cadmium(II)-substituted Phe171Asp/Glu219Ala double mutant of FL-MMP- 12 Rg histogram Rg, nm
log I(s)
 s, nm-1
Macrophage metalloelastase MOLMOL model
log I(s)
 s, nm-1
Macrophage metalloelastase MOLMOL model
Synchrotron SAXS data from solutions of NNGH-inhibited, cadmium(II)-substituted Phe171Asp/Glu219Ala double mutant of FL-MMP- 12 in 20 mM Tris10 mM CaCl2, 0.3 M NaCl, 0.2 M AHA, pH 7.2 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.8 and 8.3 mg/ml were measured . Two successive 120 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Tags: X33
Macrophage metalloelastase (FL-MMP-12)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   54.0 kDa
 
UniProt   P39900
Sequence   FASTA