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2BE9

Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius

Summary for 2BE9
Entry DOI10.2210/pdb2be9/pdb
Related1PG5
DescriptorAspartate carbamoyltransferase, Aspartate carbamoyltransferase regulatory chain, ZINC ION, ... (6 entities in total)
Functional Keywordsatcase, hyperthermophilic, temperature, transferase, allosteric, holoenzyme, ctp complex
Biological sourceSulfolobus acidocaldarius
More
Total number of polymer chains2
Total formula weight53822.29
Authors
De Vos, D.,Savvides, S.N.,Van Beeumen, J.J. (deposition date: 2005-10-23, release date: 2006-10-31, Last modification date: 2023-08-23)
Primary citationDe Vos, D.,Xu, Y.,Aerts, T.,Van Petegem, F.,Van Beeumen, J.J.
Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP.
Biochem.Biophys.Res.Commun., 372:40-44, 2008
Cited by
PubMed Abstract: Aspartate carbamoyltransferase (ATCase) is a paradigm for allosteric regulation of enzyme activity. B-class ATCases display very similar homotropic allosteric behaviour, but differ extensively in their heterotropic patterns. The ATCase from the thermoacidophilic archaeon Sulfolobus acidocaldarius, for example, is strongly activated by its metabolic pathway's end product CTP, in contrast with Escherichia coli ATCase which is inhibited by CTP. To investigate the structural basis of this property, we have solved the crystal structure of the S. acidocaldarius enzyme in complex with CTP. Structure comparison reveals that effector binding does not induce similar large-scale conformational changes as observed for the E. coli ATCase. However, shifts in sedimentation coefficients upon binding of the bi-substrate analogue PALA show the existence of structurally distinct allosteric states. This suggests that the so-called "Nucleotide-Perturbation model" for explaining heterotropic allosteric behaviour, which is based on global conformational strain, is not a general mechanism of B-class ATCases.
PubMed: 18477471
DOI: 10.1016/j.bbrc.2008.04.173
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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