6V0T
Crystal Structure of Catalytic Subunit of Bovine Pyruvate Dehydrogenase Phosphatase 1 - Catalytic Domain
Replaces: 3N3CSummary for 6V0T
| Entry DOI | 10.2210/pdb6v0t/pdb |
| Descriptor | [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial, MANGANESE (II) ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | pyruvate dehydrogenase phosphatase, pyruvate dehydrogenase, transferase, hydrolase |
| Biological source | Bos taurus (Bovine) |
| Total number of polymer chains | 1 |
| Total formula weight | 53147.96 |
| Authors | Guo, Y.,Qiu, W.,Ernst, S.R.,Carroll, D.W.,Hackert, M.L. (deposition date: 2019-11-19, release date: 2019-12-18, Last modification date: 2023-10-11) |
| Primary citation | Guo, Y.,Qiu, W.,Roche, T.E.,Hackert, M.L. Crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase. Acta Crystallogr.,Sect.F, 76:292-301, 2020 Cited by PubMed Abstract: Mammalian pyruvate dehydrogenase (PDH) activity is tightly regulated by phosphorylation and dephosphorylation, which is catalyzed by PDH kinase isomers and PDH phosphatase isomers, respectively. PDH phosphatase isomer 1 (PDP1) is a heterodimer consisting of a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r). Here, the crystal structure of bovine PDP1c determined at 2.1 Å resolution is reported. The crystals belonged to space group P321, with unit-cell parameters a = b = 75.3, c = 173.2 Å. The structure was solved by molecular-replacement methods and refined to a final R factor of 21.9% (R = 24.7%). The final model consists of 402 of a possible 467 amino-acid residues of the PDP1c monomer, two Mn ions in the active site, an additional Mn ion coordinated by His410 and His414, two MnSO ion pairs at special positions near the crystallographic twofold symmetry axis and 226 water molecules. Several new features of the PDP1c structure are revealed. The requirements are described and plausible bases are deduced for the interaction of PDP1c with PDP1r and other components of the pyruvate dehydrogenase complex. PubMed: 32627744DOI: 10.1107/S2053230X20007943 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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