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ACT domain

Self-stabilizing region of a metabolic protein

Self-stabilizing region of a metabolic protein

FieldValue
SymbolACT
NameACT
imagePDB 2j0w EBI.jpg
captionCrystal structure of E. coli aspartokinase iii in complex with aspartate and adp (r-state)
PfamPF01842
Pfam_clanCL0070
InterProIPR002912
SCOP1psd
CDDcd02116

In molecular biology, the ACT domain is a protein domain that is found in a variety of proteins involved in metabolism. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. A pair of ACT domains form an eight-stranded antiparallel sheet with two molecules of allosteric inhibitor serine bound in the interface. Biochemical exploration of a few other proteins containing ACT domains supports the suggestions that these domains contain the archetypical ACT structure.

The ACT domain was discovered by Aravind and Koonin using iterative sequence searches.

References

References

  1. (December 2001). "The ACT domain family". Current Opinion in Structural Biology.
  2. (April 1999). "Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches". Journal of Molecular Biology.
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