4MTU
beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum
Summary for 4MTU
| Entry DOI | 10.2210/pdb4mtu/pdb |
| Related | 4MZQ |
| Descriptor | Beta-alanyl-CoA:ammonia lyase 2, ZINC ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | hot dog fold, lyase |
| Biological source | Clostridium propionicum |
| Total number of polymer chains | 1 |
| Total formula weight | 16185.67 |
| Authors | Heine, A.,Reuter, K. (deposition date: 2013-09-20, release date: 2014-03-26, Last modification date: 2024-02-28) |
| 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 Cited by 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: 24623648DOI: 10.1002/prot.24557 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.97 Å) |
Structure validation
Download full validation report
