1T4D
Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase (EcASADH), at 1.95 Angstrom resolution
Summary for 1T4D
| Entry DOI | 10.2210/pdb1t4d/pdb |
| Related | 1T4B |
| Descriptor | Aspartate-semialdehyde dehydrogenase (2 entities in total) |
| Functional Keywords | asadh, aspartate semialdehyde dehydrogenase, hosr, lysine biosynthesis, nadp+ oxidoreductase (phosphorylating), domain movement, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 120167.06 |
| Authors | Nichols, C.E.,Dhaliwal, B.,Lockyer, M.,Hawkins, A.R.,Stammers, D.K. (deposition date: 2004-04-29, release date: 2004-08-17, Last modification date: 2023-08-23) |
| Primary citation | Nichols, C.E.,Dhaliwal, B.,Lockyer, M.,Hawkins, A.R.,Stammers, D.K. 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, 2004 Cited by PubMed 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. PubMed: 15288787DOI: 10.1016/j.jmb.2004.05.073 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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