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TitleQuaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.
Journal, issue, pagesJ Biol Chem, Vol. 294, Issue 30, Page 11609-11621, Year 2019
Publish dateJul 26, 2019
AuthorsYu Yang / Ian Davis / Tsutomu Matsui / Ivan Rubalcava / Aimin Liu /
PubMed Abstractα-Amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) plays an important role in l-tryptophan degradation via the kynurenine pathway. ACMSD forms a homodimer and is functionally inactive ...α-Amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) plays an important role in l-tryptophan degradation via the kynurenine pathway. ACMSD forms a homodimer and is functionally inactive as a monomer because its catalytic assembly requires an arginine residue from a neighboring subunit. However, how the oligomeric state and self-association of ACMSD are controlled in solution remains unexplored. Here, we demonstrate that ACMSD from can self-assemble into homodimer, tetramer, and higher-order structures. Using size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) analysis, we investigated the ACMSD tetramer structure, and fitting the SAXS data with X-ray crystal structures of the monomeric component, we could generate a pseudo-atomic structure of the tetramer. This analysis revealed a tetramer model of ACMSD as a head-on dimer of dimers. We observed that the tetramer is catalytically more active than the dimer and is in equilibrium with the monomer and dimer. Substituting a critical residue of the dimer-dimer interface, His-110, altered the tetramer dissociation profile by increasing the higher-order oligomer portion in solution without changing the X-ray crystal structure. ACMSD self-association was affected by pH, ionic strength, and other electrostatic interactions. Alignment of ACMSD sequences revealed that His-110 is highly conserved in a few bacteria that utilize nitrobenzoic acid as a sole source of carbon and energy, suggesting a dedicated functional role of ACMSD's self-assembly into the tetrameric and higher-order structures. These results indicate that the dynamic oligomerization status potentially regulates ACMSD activity and that SEC-SAXS coupled with X-ray crystallography is a powerful tool for studying protein self-association.
External linksJ Biol Chem / PubMed:31189654 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.77 - 3.131 Å
Structure data

SASDFM5:
Mutant 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, H110A tetramer, at pH 8.5
Method: SAXS/SANS

SASDFN5:
Wild type 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, ACMSD tetramer, at pH 7.0
Method: SAXS/SANS

PDB-6mgs:
Crystal structure of alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde-Decarboxylase with Space Group of C2221
Method: X-RAY DIFFRACTION / Resolution: 3.131 Å

PDB-6mgt:
Crystal structure of alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde Decarboxylase Mutant H110A
Method: X-RAY DIFFRACTION / Resolution: 2.77 Å

Chemicals

ChemComp-CO:
Unknown entry

ChemComp-HOH:
WATER

Source
  • pseudomonas fluorescens (bacteria)
KeywordsLYASE / Holo structure / decarboxylase

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