5VIT

Crystal structure of a Pseudomonas malonate decarboxylase hetero-tetramer in complex with malonate

Summary for 5VIT

• Entry DOI: 10.2210/pdb5vit/pdb
• Related: 5VIP 5VJ1
• Descriptor: MdcA, MdcC, MdcD, ... (6 entities in total)
• Functional Keywords: acyl carrier protein, acetyl-coa carboxylase, transferase
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); More
• Cellular location: Cytoplasm : Q4K4F7 A0A071KS24
• Total number of polymer chains: 16
• Total formula weight: 532076.78

Authors

Maderbocus, R.,Tong, L. (deposition date: 2017-04-17, release date: 2017-08-16, Last modification date: 2024-03-13)

Primary citation

Maderbocus, R.,Fields, B.L.,Hamilton, K.,Luo, S.,Tran, T.H.,Dietrich, L.E.P.,Tong, L.
Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer.
Nat Commun, 8:160-160, 2017

PubMed Abstract: Pseudomonas species and other aerobic bacteria have a biotin-independent malonate decarboxylase that is crucial for their utilization of malonate as the sole carbon and energy source. The malonate decarboxylase holoenzyme contains four subunits, having an acyl-carrier protein (MdcC subunit) with a distinct prosthetic group, as well as decarboxylase (MdcD-MdcE) and acyl-carrier protein transferase (MdcA) catalytic activities. Here we report the crystal structure of a Pseudomonas malonate decarboxylase hetero-tetramer, as well as biochemical and functional studies based on the structural information. We observe a malonate molecule in the active site of MdcA and we also determine the structure of malonate decarboxylase with CoA in the active site of MdcD-MdcE. Both structures provide molecular insights into malonate decarboxylase catalysis. Mutations in the hetero-tetramer interface can abolish holoenzyme formation. Mutations in the hetero-tetramer interface and the active sites can abolish Pseudomonas aeruginosa growth in a defined medium with malonate as the sole carbon source.Some aerobic bacteria contain a biotin-independent malonate decarboxylase (MDC), which allows them to use malonate as the sole carbon source. Here, the authors present the crystal structure of a Pseudomonas MDC and give insights into its catalytic mechanism and function.

PubMed: 28757619
DOI: 10.1038/s41467-017-00233-z

Experimental method

X-RAY DIFFRACTION (2.203 Å)