We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

6d97

From Proteopedia

Jump to: navigation, search

Structure of aldehyde dehydrogenase 12 (ALDH12) from Zea mays

Structural highlights

6d97 is a 4 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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