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J. Biol. Chem., Vol. 259, Issue 23, 14458-14462, 12, 1984

Molecular structure of trimethylamine dehydrogenase from the bacterium W3A1 at 6.0-A resolution

LW Lim, N Shamala, FS Mathews and DJ Steenkamp

An electron density map of trimethylamine dehydrogenase has been calculated at 6.0-A resolution. Protein phases were based on two isomorphous mercury derivatives with similar binding properties, and on anomalous scattering measurements. The map has been averaged about the noncrystallographic 2-fold axis, plotted on transparent sheets and used to construct a wooden model. The elipsoidal dimer has a large inter- subunit interface. Each subunit appears to contain three closely associated domains with the iron-sulfur cluster located between two of them. The map suggests an alpha/beta-structure for two of the domains and a large helix content for the third.
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