7CIJ
Crystal structure of L-methionine decarboxylase from Streptomyces sp.590 in complexed with 3-methlythiopropylamine (external aldimine form).
Summary for 7CIJ
| Entry DOI | 10.2210/pdb7cij/pdb |
| Descriptor | L-methionine decarboxylase, [6-methyl-4-[(E)-3-methylsulfanylpropyliminomethyl]-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate (3 entities in total) |
| Functional Keywords | decarboxylase, plp-dependent enzymes, lyase |
| Biological source | Streptomyces sp. 590 KI-2014 |
| Total number of polymer chains | 2 |
| Total formula weight | 123622.85 |
| Authors | Okawa, A.,Shiba, T.,Hayashi, M.,Onoue, Y.,Murota, M.,Sato, D.,Inagaki, J.,Tamura, T.,Harada, S.,Inagaki, K. (deposition date: 2020-07-07, release date: 2021-01-27, Last modification date: 2023-11-29) |
| Primary citation | Okawa, A.,Shiba, T.,Hayashi, M.,Onoue, Y.,Murota, M.,Sato, D.,Inagaki, J.,Tamura, T.,Harada, S.,Inagaki, K. Structural basis for substrate specificity of l-methionine decarboxylase. Protein Sci., 30:663-677, 2021 Cited by PubMed Abstract: l -Methionine decarboxylase (MetDC) from Streptomyces sp. 590 is a vitamin B -dependent enzyme and catalyzes the non-oxidative decarboxylation of l -methionine to produce 3-methylthiopropylamine and carbon dioxide. We present here the crystal structures of the ligand-free form of MetDC and of several enzymatic reaction intermediates. Group II amino acid decarboxylases have many residues in common around the active site but the residues surrounding the side chain of the substrate differ. Based on information obtained from the crystal structure, and mutational and biochemical experiments, we propose a key role for Gln64 in determining the substrate specificity of MetDC, and for Tyr421 as the acid catalyst that participates in protonation after the decarboxylation reaction. PubMed: 33452696DOI: 10.1002/pro.4027 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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