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5OU5

Crystal structure of maize chloroplastic photosynthetic NADP(+)-dependent malic enzyme

Summary for 5OU5
Entry DOI10.2210/pdb5ou5/pdb
DescriptorMalic enzyme, SODIUM ION, POTASSIUM ION, ... (4 entities in total)
Functional Keywordsmalic enzyme, oxidative decarboxylase, nadp-dependent, c4 photsynthesis, photosynthesis
Biological sourceZea mays (Maize)
Total number of polymer chains4
Total formula weight254984.42
Authors
Bovdilova, A.,Hoeppner, A.,Maurino, V.G. (deposition date: 2017-08-23, release date: 2018-12-12, Last modification date: 2024-05-08)
Primary citationAlvarez, C.E.,Bovdilova, A.,Hoppner, A.,Wolff, C.C.,Saigo, M.,Trajtenberg, F.,Zhang, T.,Buschiazzo, A.,Nagel-Steger, L.,Drincovich, M.F.,Lercher, M.J.,Maurino, V.G.
Molecular adaptations of NADP-malic enzyme for its function in C4photosynthesis in grasses.
Nat.Plants, 5:755-765, 2019
Cited by
PubMed Abstract: In C grasses of agronomical interest, malate shuttled into the bundle sheath cells is decarboxylated mainly by nicotinamide adenine dinucleotide phosphate (NADP)-malic enzyme (C-NADP-ME). The activity of C-NADP-ME was optimized by natural selection to efficiently deliver CO to Rubisco. During its evolution from a plastidic non-photosynthetic NADP-ME, C-NADP-ME acquired increased catalytic efficiency, tetrameric structure and pH-dependent inhibition by its substrate malate. Here, we identified specific amino acids important for these C adaptions based on strict differential conservation of amino acids, combined with solving the crystal structures of maize and sorghum C-NADP-ME. Site-directed mutagenesis and structural analyses show that Q503, L544 and E339 are involved in catalytic efficiency; E339 confers pH-dependent regulation by malate, F140 is critical for the stabilization of the oligomeric structure and the N-terminal region is involved in tetramerization. Together, the identified molecular adaptations form the basis for the efficient catalysis and regulation of one of the central biochemical steps in C metabolism.
PubMed: 31235877
DOI: 10.1038/s41477-019-0451-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

246031

数据于2025-12-10公开中

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