4MZQ

beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum in complex with propionyl-CoA

Summary for 4MZQ

• Entry DOI: 10.2210/pdb4mzq/pdb
• Related: 4MTU
• Descriptor: beta-Alanyl-CoA:Ammonia Lyase, propionyl Coenzyme A (3 entities in total)
• Functional Keywords: hot dog fold, lyase
• Biological source: Clostridium propionicum
• Total number of polymer chains: 12
• Total formula weight: 202173.55

Authors

Heine, A.,Reuter, K. (deposition date: 2013-09-30, release date: 2014-03-26, Last modification date: 2023-09-20)

Primary citation

Heine, A.,Herrmann, G.,Selmer, T.,Terwesten, F.,Buckel, W.,Reuter, K.
High resolution crystal structure of Clostridium propionicum beta-alanyl-CoA:ammonia lyase, a new member of the "hot dog fold" protein superfamily.
Proteins, 82:2041-2053, 2014

PubMed Abstract: Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 Å as well as in complex with CoA at a resolution of 1.59 Å. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking.

PubMed: 24623648
DOI: 10.1002/prot.24557

Experimental method

X-RAY DIFFRACTION (1.587 Å)