PF22468

ACT domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameACT_9
ClanACT
Author Bateman A;0000-0002-6982-4660 Lazaro Pinto Beatriz;0000-0001-6837-2941
Sequence Ontology0000417

Description

This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid
[1]
. This domain folds as a four-stranded antiparallel sheet with two alpha-helices parallel to the sheet and located on one side of the sheet
[2]
.

References

1.The structural basis for allosteric inhibition of a threonine-sensitive aspartokinase. Liu X, Pavlovsky AG, Viola RE. J. Biol. Chem. 283, 16216-25, (2008). View articlePMID: 18334478

2.A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase. Mas-Droux C, Curien G, Robert-Genthon M, Laurencin M, Ferrer JL, Dumas R. Plant Cell 18, 1681-92, (2006). View articlePMID: 16731588

Further reading

3. Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine. Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK. J. Biol. Chem. 281, 31544-52, (2006). View articlePMID: 16905770

4. Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus. Yoshida A, Tomita T, Kono H, Fushinobu S, Kuzuyama T, Nishiyama M. FEBS J. 276, 3124-36, (2009). View articlePMID: 19490113

5. Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum. Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M. J. Mol. Biol. 368, 521-36, (2007). View articlePMID: 17350037

6. The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase. Faehnle CR, Liu X, Pavlovsky A, Viola RE. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62, 962-6, (2006). View articlePMID: 17012784

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