Open AccessStructure of photosynthetic glyceraldehyde‐3‐phosphate dehydrogenase (isoform A 4 ) from Arabidopsis thaliana in complex with NAD
Author(s) -
Fermani Simona,
Sparla Francesca,
Marri Lucia,
Thumiger Anton,
Pupillo Paolo,
Falini Giuseppe,
Trost Paolo
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110013527
Subject(s) - tetramer , dimer , nad+ kinase , dehydrogenase , arabidopsis thaliana , crystallography , molecular replacement , chemistry , glyceraldehyde 3 phosphate dehydrogenase , protein subunit , stereochemistry , crystal structure , biochemistry , mutant , enzyme , gene , organic chemistry
The crystal structure of the A 4 isoform of photosynthetic glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) from Arabidopsis thaliana , expressed in recombinant form and complexed with NAD, is reported. The crystals, which were grown in 2.4 M ammonium sulfate and 0.1 M sodium citrate, belonged to space group I 222. The asymmetric unit includes ten subunits, i.e. two independent tetramers plus a dimer that generates a third tetramer by a crystallographic symmetry operation. The crystal structure was solved by molecular replacement and refined to an R factor of 23.7% and an R free factor of 28.9% at 2.6 Å resolution. In the final model, each subunit binds one NAD + molecule and two sulfates, which occupy the P s and the P i anion‐binding sites. Detailed knowledge of this structure is instrumental for structural investigation of supramolecular complexes of A 4 ‐GAPDH, phosphoribulokinase and CP12, which are involved in the regulation of photosynthesis in the model plant A. thaliana .