1NI4
HUMAN PYRUVATE DEHYDROGENASE
Summary for 1NI4
| Entry DOI | 10.2210/pdb1ni4/pdb |
| Descriptor | Pyruvate dehydrogenase E1 component: Alpha subunit, Pyruvate dehydrogenase E1 component: Beta subunit, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | thiamin pyrophosphate, pyruvate, alpha-keto acid dehydrogenase, pyruvate dehydrogenase, oxidoreductase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Mitochondrion matrix: P08559 P11177 |
| Total number of polymer chains | 4 |
| Total formula weight | 159444.81 |
| Authors | Ciszak, E.,Korotchkina, L.G.,Dominiak, P.M.,Sidhu, S.,Patel, M.S. (deposition date: 2002-12-20, release date: 2003-06-17, Last modification date: 2024-10-30) |
| Primary citation | Ciszak, E.M.,Korotchkina, L.G.,Dominiak, P.M.,Sidhu, S.,Patel, M.S. Structural Basis for Flip-Flop Action of Thiamin Pyrophosphate-Dependent Enzymes Revealed by Human Pyruvate Dehydrogenase J.Biol.Chem., 278:21240-21246, 2003 Cited by PubMed Abstract: The derivative of vitamin B1, thiamin pyrophosphate, is a cofactor of enzymes performing catalysis in pathways of energy production. In alpha2beta2-heterotetrameric human pyruvate dehydrogenase, this cofactor is used to cleave the Calpha-C(=O) bond of pyruvate followed by reductive acetyl transfer to lipoyl-dihydrolipoamide acetyltransferase. The dynamic nonequivalence of two, otherwise chemically equivalent, catalytic sites has not yet been understood. To understand the mechanism of action of this enzyme, we determined the crystal structure of the holo-form of human pyruvate dehydrogenase at 1.95-A resolution. We propose a model for the flip-flop action of this enzyme through a concerted approximately 2-A shuttle-like motion of its heterodimers. Similarity of thiamin pyrophosphate binding in human pyruvate dehydrogenase with functionally related enzymes suggests that this newly defined shuttle-like motion of domains is common to the family of thiamin pyrophosphate-dependent enzymes. PubMed: 12651851DOI: 10.1074/jbc.M300339200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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