5n5s | pdb_00005n5s

Crystal structure of aldehyde dehydrogenase 21 (ALDH21) from Physcomitrella patens in complex with NADP+

spinqualitylabelsall models 5n5s, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n5s is a 4 chain structure with sequence from Physcomitrium patens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: EDO, NAP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A9SS48_PHYPA Publication Abstract from PubMed Lower plant species including some green algae, non-vascular plants (bryophytes) as well as the oldest vascular plants (lycopods) and ferns (monilophytes) possess a unique aldehyde dehydrogenase (ALDH) gene named ALDH21, which is upregulated during dehydration. However, the gene is absent in flowering plants. Here, we show that ALDH21 from the moss Physcomitrella patens codes for a tetrameric NADP+ -dependent succinic semialdehyde dehydrogenase (SSALDH), which converts succinic semialdehyde, an intermediate of the gamma-aminobutyrate (GABA) shunt pathway, into succinate in the cytosol. NAD+ is a very poor coenzyme for ALDH21 unlike for mitochondrial SSALDHs (ALDH5), which are the closest related ALDH members. Structural comparison between the apoform and the coenzyme complex reveal that NADP+ binding induces a conformational change of the loop carrying Arg-228, which seals the NADP+ in the coenzyme cavity via its 2'-phosphate and alpha-phosphate groups. The crystal structure with the bound product succinate shows that its carboxylate group establishes salt bridges with both Arg-121 and Arg-457 and a hydrogen bond with Tyr-296. While both arginine residues are pre-formed for substrate/product binding, Tyr-296 moves by more than 1 A. Both R121A and R457A variants are almost inactive demonstrating a key role of each arginine in catalysis. Our study implies that bryophytes but presumably also some green algae, lycopods and ferns, which carry both ALDH21 and ALDH5 genes, can oxidize SSAL to succinate in both cytosol and mitochondria indicating more diverse GABA shunt pathway compared with higher plants carrying only the mitochondrial ALDH5. This article is protected by copyright. All rights reserved. The ALDH21 gene found in lower plants and some vascular plants codes for a NADP+ -dependent succinic semialdehyde dehydrogenase.,Kopecna M, Vigouroux A, Vilim J, Koncitikova R, Briozzo P, Hajkova E, Jaskova L, von Schwartzenberg K, Sebela M, Morera S, Kopecny D Plant J. 2017 Jul 27. doi: 10.1111/tpj.13648. PMID:28749584 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldehyde dehydrogenase 3D structures

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