3ADA
Heterotetrameric Sarcosine Oxidase from Corynebacterium sp. U-96 in complex with sulfite
Summary for 3ADA
| Entry DOI | 10.2210/pdb3ada/pdb |
| Related | 1VRQ 1X31 3AD7 3AD8 3AD9 |
| Descriptor | SARCOSINE OXIDASE ALPHA SUBUNIT, ZINC ION, SARCOSINE OXIDASE BETA SUBUNIT, ... (11 entities in total) |
| Functional Keywords | sarcosine oxidase, ligand complex, oxidoreductase |
| Biological source | Corynebacterium sp. U-96 More |
| Total number of polymer chains | 4 |
| Total formula weight | 182081.61 |
| Authors | Suzuki, H.,Moriguchi, T.,Ida, K. (deposition date: 2010-01-15, release date: 2010-08-25, Last modification date: 2023-11-01) |
| Primary citation | Moriguchi, T.,Ida, K.,Hikima, T.,Ueno, G.,Yamamoto, M.,Suzuki, H. Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96. J.Biochem., 148:491-505, 2010 Cited by PubMed Abstract: We characterized the crystal structures of heterotetrameric sarcosine oxidase (SO) from Corynebacterium sp. U-96 complexed with methylthioacetate (MTA), pyrrole 2-carboxylate (PCA) and sulphite, and of sarcosine-reduced SO. SO comprises α-, β-, γ- and δ-subunits; FAD and FMN cofactors; and a large internal cavity. MTA and PCA are sandwiched between the re-face of the FAD isoalloxazine ring and the β-subunit C-terminal residues. Reduction of flavin cofactors shifts the β-subunit Ala1 towards the α-subunit Met55, forming a surface cavity at the oxygen-channel vestibule and rendering the β-subunit C-terminal residues mobile. We identified three channels connecting the cavity and the enzyme surface. Two of them exist in the inter-subunit space between α and β-subunits, and the substrate sarcosine seems to enter the active site through either of these channels and reaches the re-side of the FAD isoalloxazine ring by traversing the mobile β-subunit C-terminal residues. The third channel goes through the α-subunit and has a folinic acid-binding site, where the iminium intermediate is converted to Gly and either formaldehyde or, 5,10-methylenetetrahydrofolate. Oxygen molecules are probably located on the surface cavity and diffuse to the FMN isoalloxazine ring; the H(2)O(2) formed exits via the oxygen channel. PubMed: 20675294DOI: 10.1093/jb/mvq083 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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