PMID:15288787
| Citation |
Nichols, CE, Dhaliwal, B, Lockyer, M, Hawkins, AR and Stammers, DK (2004) High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase. J. Mol. Biol. 341:797-806 |
|---|---|
| Abstract |
Two high-resolution structures have been determined for Eschericia coli aspartate beta-semialdehyde dehydrogenase (ecASADH), an enzyme of the aspartate biosynthetic pathway, which is a potential target for novel antimicrobial drugs. Both ASADH structures were of the open form and were refined to 1.95 A and 1.6 A resolution, allowing a more detailed comparison with the closed form of the enzyme than previously possible. A more complex scheme for domain closure is apparent with the subunit being split into two further sub-domains with relative motions about three hinge axes. Analysis of hinge data and torsion-angle difference plots is combined to allow the proposal of a detailed structural mechanism for ecASADH domain closure. Additionally, asymmetric distortions of individual subunits are identified, which form the basis for the previously reported "half-of-the-sites reactivity" (HOSR). A putative explanation of this arrangement is also presented, suggesting the HOSR system may provide a means for ecASADH to offset the energy required to remobilise flexible loops at the end of the reaction cycle, and hence avoid falling into an energy minimum. |
| Links |
PubMed Online version:10.1016/j.jmb.2004.05.073 |
| Keywords |
Aspartate-Semialdehyde Dehydrogenase/chemistry; Binding Sites; Crystallography, X-Ray; Databases as Topic; Dimerization; Escherichia coli/enzymology; Models, Chemical; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary |
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