Murthy, M. R. N. ; Michael Garavito, R. ; John Johnson, E. ; Michael Rossmann, G. (1980) Structure of lobster apo-D-glyceraldehyde-3-phosphate dehydrogenase at 3.0 Å resolution Journal of Molecular Biology, 138 (4). pp. 859-872. ISSN 0022-2836
Full text not available from this repository.
Official URL: http://www.sciencedirect.com/science/article/pii/0...
Related URL: http://dx.doi.org/10.1016/0022-2836(80)90069-8
Abstract
Lobster apo-glyceraldehyde-3-phosphate dehydrogenase was prepared by first lowering the pH to 4.8, thus reducing the NAD binding energy, and then separating the enzyme and coenzyme on a Sephadex column. Triclinic crystals were grown from an ammonium sulfate solution at pH 6.2. The apo-structure was initially determined approximately by comparison with the known hologlyceraldehyde-3-phosphate dehydrogenase molecule. The former was then refined using the 222 molecular symmetry with the molecular replacement technique. Only minor conformational differences were observed between apo and holo-glyceraldehyde-3-phosphate dehydrogenase. Trp193 in the "S loop" and the adenine-binding pocket showed the most significant changes.
Item Type: | Article |
---|---|
Source: | Copyright of this article belongs to Elsevier Science. |
ID Code: | 74843 |
Deposited On: | 19 Dec 2011 12:13 |
Last Modified: | 19 Dec 2011 12:13 |
Repository Staff Only: item control page