7BZV

Crystal structure of 2-aminomuconic 6-semialdehyde dehydrogenase from Pseudomonas species AP-3

Summary for 7BZV

• Entry DOI: 10.2210/pdb7bzv/pdb
• Descriptor: 2-aminomuconic 6-semialdehyde dehydrogenase, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: meta-cleavage pathway for 2-aminophenol catabolism. 2-aminomuconic 6-semialdehyde dehydrogenase, biosynthetic protein
• Biological source: Pseudomonas sp.
• Total number of polymer chains: 2
• Total formula weight: 108644.99

Authors

Shi, Q.L.,Chen, Y.J.,Su, D. (deposition date: 2020-04-28, release date: 2021-04-28, Last modification date: 2024-06-19)

Primary citation

Shi, Q.,Chen, Y.,Li, X.,Dong, H.,Chen, C.,Zhong, Z.,Yang, C.,Liu, G.,Su, D.
The tetrameric assembly of 2-aminomuconic 6-semialdehyde dehydrogenase is a functional requirement of cofactor NAD + binding.
Environ.Microbiol., 2021

PubMed Abstract: The bacterium Pseudomonas sp. AP-3 is able to use the environmental pollutant 2-aminophenol as its sole source of carbon, nitrogen, and energy. Eight genes (amnA, B, C, D, E, F, G, and H) encoding 2-aminophenol metabolizing enzymes are clustered into a single operon. 2-Aminomuconic 6-semialdehyde dehydrogenase (AmnC), a member of the aldehyde dehydrogenase (ALDH) superfamily, is responsible for oxidizing 2-aminomuconic 6-semialdehyde to 2-aminomuconate. In contrast to many other members of the ALDH superfamily, the structural basis of the catalytic activity of AmnC remains elusive. Here, we present the crystal structure of AmnC, which displays a homotetrameric quaternary assembly that is directly involved in its enzymatic activity. The tetrameric state of AmnC in solution was also presented using small-angle X-ray scattering. The tetramerization of AmnC is mediated by the assembly of a protruding hydrophobic beta-strand motif and residues V121 and S123 located in the NAD -binding domain of each subunit. Dimeric mutants of AmnC dramatically lose NAD binding affinity and failed to oxidize the substrate analogue 2-hydroxymuconate-6-semialdehyde to α-hydroxymuconic acid, indicating that tetrameric assembly of AmnC is functional requirement.

PubMed: 34806815
DOI: 10.1111/1462-2920.15840

Experimental method

X-RAY DIFFRACTION (1.988 Å)