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Journal Article

Two conformations of crystalline adenylate kinase


Sachsenheimer,  W.
Max Planck Institute for Medical Research, Max Planck Society;


Schulz,  G. E.
Max Planck Institute for Medical Research, Max Planck Society;

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Sachsenheimer, W., & Schulz, G. E. (1977). Two conformations of crystalline adenylate kinase. Journal of Molecular Biology (London), 114(1), 23-36. doi:10.1016/0022-2836(77)90280-7.

Cite as: https://hdl.handle.net/21.11116/0000-0002-D60A-2
Pig muscle adenylate kinase (EC2.7.4.3) can exist in three crystal forms, which are interconvertible. For crystal form A the enzyme structure is known in atomic detail. We report the X-ray diffraction analysis of crystal form B at 4.7 Å resolution and a comparison with the A form. During the transition from A to B the packing arrangement of the molecules changes slightly. Moreover, the individual molecule undergoes an appreciable conformational change: by displacing a chain segment of seven residues and two adjacent α-helices a hydrophobic pocket is opened deep in the cleft near the centre of the molecule. Concomitantly the β-pleated sheet is enlarged by about four hydrogen bonds in the B form. Several lines of evidence indicate that the observed conformational change is an intrinsic property of the molecule and is not induced by crystal packing forces.