6JVW
Crystal structure of maleylpyruvate hydrolase from Sphingobium sp. SYK-6 in complex with manganese (II) ion and pyruvate
Summary for 6JVW
| Entry DOI | 10.2210/pdb6jvw/pdb |
| Descriptor | maleylpyruvate hydrolase, PYRUVIC ACID, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Sphingobium sp. (strain NBRC 103272 / SYK-6) |
| Total number of polymer chains | 2 |
| Total formula weight | 67074.44 |
| Authors | Hong, H.,Kim, K.-J. (deposition date: 2019-04-17, release date: 2019-05-29, Last modification date: 2023-11-22) |
| Primary citation | Hong, H.,Seo, H.,Kim, K.J. Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls. Biochem.Biophys.Res.Commun., 514:765-771, 2019 Cited by PubMed Abstract: Sphingobium sp. strain SYK-6, an aerobic gram-negative bacillus found in soil, is known for utilizing lignin-derived monoaryls and biaryls as carbon sources and degrading aromatic compounds. The Sphingobium sp. strain SYK-6 genome contains three genes involved in salicylate catabolism: SLG_11260, SLG_11270, and SLG_11280. Here, we report that the gene product of SLG_11280 functions as a maleylpyruvate hydrolase (SsMPH) with K and K values of 166.2 μM and 3.76 min, respectively. This study also reveals the crystal structures of both the apo and pyruvate-manganese ion-bound SsMPH, which revealed that like other fumarylacetoacetate hydrolases, SsMPH dimerizes and has nine unique 3-helices. Molecular docking studies of maleylpyruvate also revealed the likely binding mode of SsMPH and its substrate. PubMed: 31079929DOI: 10.1016/j.bbrc.2019.05.030 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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