1t4b
From Proteopedia
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'''1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.''' | '''1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.''' | ||
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[[Category: Nichols, C E.]] | [[Category: Nichols, C E.]] | ||
[[Category: Stammers, D K.]] | [[Category: Stammers, D K.]] | ||
| - | [[Category: | + | [[Category: Asadh]] |
| - | [[Category: | + | [[Category: Aspartate semialdehyde dehydrogenase]] |
| - | [[Category: | + | [[Category: Domain movement]] |
| - | [[Category: | + | [[Category: Hosr]] |
| - | [[Category: | + | [[Category: Lysine biosynthesis]] |
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Revision as of 06:30, 3 May 2008
1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.
Overview
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.
About this Structure
1T4B is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase., Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK, J Mol Biol. 2004 Aug 13;341(3):797-806. PMID:15288787 Page seeded by OCA on Sat May 3 09:30:29 2008
