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Protein Science (2007), 16:485-493. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Domain motions of glucosamine-6P synthase: Comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation

Stéphane Mouilleron1,2,3 and Béatrice Golinelli-Pimpaneau1

1 Laboratoire d'Enzymologie et Biochimie Structurales, Bâtiment 34, CNRS, 91198 Gif-sur-Yvette Cedex, France
2 Institut de Chimie des Substances Naturelles, UPR 2301, CNRS, 91198 Gif-sur-Yvette Cedex, France

(RECEIVED October 2, 2006; FINAL REVISION November 21, 2006; ACCEPTED December 4, 2006)

Glucosamine-6-phosphate synthase channels ammonia over 18 Å from glutamine at the glutaminase site to fructose-6P at the synthase site. We have modeled the anisotropic displacements of the glutaminase and synthase domains from the two crystallized states, the enzyme in complex with fructose-6P or in complex with glucose-6P and a glutamine affinity analog, using TLS (rigid-body motion in terms of translation, libration, and screw motions) refinement implemented in REFMAC. The domains displacements in the crystal lattices are compared to the movement of the glutaminase domain relative to the synthase domain that occurs during the catalytic cycle upon glutamine binding, which was visualized by comparing the two structures. This movement was analyzed by the program DYNDOM as a 22.8° rotation around an effective hinge axis running approximately parallel to helix 300–317 of the synthase domain, the glutaminase loop that covers the glutaminase site upon glutamine binding acting as the mechanical hinge.

Keywords: dynamic domains; hinge-bending domain motion; domain movement; translation-libration-screw refinement; anisotropic temperature factor


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Copyright © 2007 by The Protein Society.