7LB5
Pyridoxal 5'-phosphate synthase-like subunit PDX1.2 (Arabidopsis thaliana)
Summary for 7LB5
| Entry DOI | 10.2210/pdb7lb5/pdb |
| EMDB information | 23263 23264 |
| Descriptor | Pyridoxal 5'-phosphate synthase-like subunit PDX1.2 (1 entity in total) |
| Functional Keywords | pseudoenzyme, dodecamer, vitamin b6, plant protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 12 |
| Total formula weight | 448896.05 |
| Authors | Novikova, I.V.,Evans, J.E. (deposition date: 2021-01-07, release date: 2021-09-22, Last modification date: 2024-05-29) |
| Primary citation | Novikova, I.V.,Zhou, M.,Du, C.,Parra, M.,Kim, D.N.,VanAernum, Z.L.,Shaw, J.B.,Hellmann, H.,Wysocki, V.H.,Evans, J.E. Tunable Heteroassembly of a Plant Pseudoenzyme-Enzyme Complex. Acs Chem.Biol., 16:2315-2325, 2021 Cited by PubMed Abstract: Pseudoenzymes have emerged as key regulatory elements in all kingdoms of life despite being catalytically nonactive. Yet many factors defining why one protein is active while its homologue is inactive remain uncertain. For pseudoenzyme-enzyme pairs, the similarity of both subunits can often hinder conventional characterization approaches. In plants, a pseudoenzyme, PDX1.2, positively regulates vitamin B production by association with its active catalytic homologues such as PDX1.3 through an unknown assembly mechanism. Here we used an integrative experimental approach to learn that such pseudoenzyme-enzyme pair associations result in heterocomplexes of variable stoichiometry, which are unexpectedly tunable. We also present the atomic structure of the PDX1.2 pseudoenzyme as well as the population averaged PDX1.2-PDX1.3 pseudoenzyme-enzyme pair. Finally, we dissected hetero-dodecamers of each stoichiometry to understand the arrangement of monomers in the heterocomplexes and identified symmetry-imposed preferences in PDX1.2-PDX1.3 interactions. Our results provide a new model of pseudoenzyme-enzyme interactions and their native heterogeneity. PubMed: 34520180DOI: 10.1021/acschembio.1c00475 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.16 Å) |
Structure validation
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