Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structural Studies of Yeast Î”(1)-pyrroline-5-carboxylate Dehydrogenase (aka ALDH4A1): Active Site Flexibility and Oligomeric State.

Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ

The proline catabolic enzyme Î”(1)-pyrroline-5-carboxylate dehydrogenase (aka ALDH4A1) catalyzes the NAD(+)-dependent oxidation of Î³-glutamate semialdehyde to L-glutamate. In Saccharomyces cerevisiae, ALDH4A1 is encoded by the PUT2 gene and known as Put2p. Here we report the steady-state kinetic parameters of the purified recombinant enzyme, two crystal structures of Put2p, and the determination of the oligomeric state and quaternary structure from small-angle ... [more]

Biochemistry Feb. 06, 2014; 0(0); [Pubmed: 24502590]

Throughput

Low Throughput

Additional Notes

dimer

Curated By

BioGRID

Interaction Summary

ALDH4A1

Gene Ontology Biological Process

Gene Ontology Molecular Function

1-pyrroline-5-carboxylate dehydrogenase activity [EXP]aldehyde dehydrogenase (NAD) activity [TAS]electron carrier activity [TAS]identical protein binding [IPI]

Gene Ontology Cellular Component