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| | ==Structure of aldehyde dehydrogenase 12 (ALDH12) from Zea mays== | | ==Structure of aldehyde dehydrogenase 12 (ALDH12) from Zea mays== |
| - | <StructureSection load='6d97' size='340' side='right' caption='[[6d97]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='6d97' size='340' side='right'caption='[[6d97]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6d97]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D97 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d97]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D97 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-glutamate_gamma-semialdehyde_dehydrogenase L-glutamate gamma-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.88 1.2.1.88] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6d97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d97 OCA], [http://pdbe.org/6d97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d97 RCSB], [http://www.ebi.ac.uk/pdbsum/6d97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d97 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d97 OCA], [https://pdbe.org/6d97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d97 RCSB], [https://www.ebi.ac.uk/pdbsum/6d97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d97 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A2H4PMI3_MAIZE A0A2H4PMI3_MAIZE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6d97" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6d97" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: L-glutamate gamma-semialdehyde dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Kopecny, D]] | + | [[Category: Zea mays]] |
| - | [[Category: Korasick, D A]] | + | [[Category: Kopecny D]] |
| - | [[Category: Tanner, J J]] | + | [[Category: Korasick DA]] |
| - | [[Category: Aldh12]] | + | [[Category: Tanner JJ]] |
| - | [[Category: L-glutamate-gamma-semialdehyde dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
A0A2H4PMI3_MAIZE
Publication Abstract from PubMed
Heterokonts, Alveolata protists, green algae from Charophyta and Chlorophyta divisions, and all Embryophyta plants possess an aldehyde dehydrogenase (ALDH) gene named ALDH12. Here, we provide a biochemical characterization of two ALDH12 family members from the lower plant Physcomitrella patens and higher plant Zea mays. We show that ALDH12 encodes an NAD(+)-dependent glutamate gamma-semialdehyde dehydrogenase (GSALDH), which irreversibly converts glutamate gamma-semialdehyde (GSAL), a mitochondrial intermediate of the proline and arginine catabolism, to glutamate. Sedimentation equilibrium and small-angle X-ray scattering analyses reveal that in solution both plant GSALDHs exist as equilibrium between a domain-swapped dimer and the dimer-of-dimers tetramer. Plant GSALDHs share very low-sequence identity with bacterial, fungal, and animal GSALDHs (classified as ALDH4), which are the closest related ALDH superfamily members. Nevertheless, the crystal structure of ZmALDH12 at 2.2-A resolution shows that nearly all key residues involved in the recognition of GSAL are identical to those in ALDH4, indicating a close functional relationship with ALDH4. Phylogenetic analysis suggests that the transition from ALDH4 to ALDH12 occurred during the evolution of the endosymbiotic plant ancestor, prior to the evolution of green algae and land plants. Finally, ALDH12 expression in maize and moss is downregulated in response to salt and drought stresses, possibly to maintain proline levels. Taken together, these results provide molecular insight into the biological roles of the plant ALDH12 family.
Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.,Korasick DA, Koncitikova R, Kopecna M, Hajkova E, Vigouroux A, Morera S, Becker DF, Sebela M, Tanner JJ, Kopecny D J Mol Biol. 2018 Dec 21. pii: S0022-2836(18)31047-7. doi:, 10.1016/j.jmb.2018.12.010. PMID:30580036[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Korasick DA, Koncitikova R, Kopecna M, Hajkova E, Vigouroux A, Morera S, Becker DF, Sebela M, Tanner JJ, Kopecny D. Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 2018 Dec 21. pii: S0022-2836(18)31047-7. doi:, 10.1016/j.jmb.2018.12.010. PMID:30580036 doi:http://dx.doi.org/10.1016/j.jmb.2018.12.010
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