Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.

Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
J Biol Chem 294(30):11609-11621 (2019 Jul 26)
PMID: 31189654
doi: 10.1074/jbc.RA119.009035 		Submitted to SASBDB: 2019 Apr 23
Published in SASBDB:

SASDFM5 – Mutant 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, H110A tetramer, at pH 8.5

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 50 mM Tris, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jul 15
RgGuinier 5.2 nm
Dmax 19.0 nm
VolumePorod 238 nm3

SASDFN5 – Wild type 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, ACMSD tetramer, at pH 7.0

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 25 mM HEPES, 5 mM DTT, pH: 7
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jan 10
RgGuinier 4.7 nm
Dmax 17.5 nm
VolumePorod 195 nm3