The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis

Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
ACS Catalysis (2020 Jun 02)

doi: 10.1021/acscatal.0c01623 		Submitted to SASBDB: 2019 Jun 18
Published in SASBDB:

SASDFY7 – Aquifex aeolicus McoA metaloxidase

Aquifex aeolicus McoA metaloxidase experimental SAS data
DAMFILT model
Sample: Aquifex aeolicus McoA metaloxidase monomer, 55 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Apr 15
RgGuinier 2.3 nm
Dmax 7.5 nm
VolumePorod 79 nm3

SASDFX7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆337-346 (MCoA∆337-346)

Aquifex aeolicus McoA metaloxidase ∆337-346 experimental SAS data
DAMMIF model
Sample: Aquifex aeolicus McoA metaloxidase ∆337-346 monomer, 54 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Dec 4
RgGuinier 2.3 nm
Dmax 7.0 nm
VolumePorod 78 nm3

SASDFW7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆328-352 (MCoA∆328-352)

Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) experimental SAS data
DAMFILT model
Sample: Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) monomer, 53 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 13
RgGuinier 2.3 nm
Dmax 6.9 nm
VolumePorod 77 nm3