1I5O
CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE
Summary for 1I5O
| Entry DOI | 10.2210/pdb1i5o/pdb |
| Related | 5at1 6at1 |
| Descriptor | ASPARTATE TRANSCARBAMOYLASE CATALYTIC CHAIN, ASPARTATE TRANSCARBAMOYLASE REGULATORY CHAIN, ZINC ION, ... (5 entities in total) |
| Functional Keywords | mutant aspartate transcarbamoylase, t-state, pala at the regulatory site, transferase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 103175.17 |
| Authors | Macol, C.P.,Tsuruta, H.,Stec, B.,Kantrowitz, E.R. (deposition date: 2001-02-28, release date: 2001-05-02, Last modification date: 2023-08-09) |
| Primary citation | Macol, C.P.,Tsuruta, H.,Stec, B.,Kantrowitz, E.R. Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase. Nat.Struct.Biol., 8:423-426, 2001 Cited by PubMed Abstract: Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state. PubMed: 11323717DOI: 10.1038/87582 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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