4ake Citations

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding.

Structure 4 147-56 (1996)
Cited: 291 times
EuropePMC logo PMID: 8805521

Abstract

Background
Results

We have solved the structure of unligated adenylate kinase from Escherichia coli at 2.2 degree resolution and compared it with the high-resolution structure of the same enzyme ligated with an inhibitor mimicking both substrates, ATP and AMP. This comparison shows that, upon substrate binding, the enzyme increases its chain mobility in a region remote from the active center. As this region 'solidifies' again on substrate release, we propose that it serves as a 'counterweight' balancing the substrate binding energy.

Reviews - 4ake mentioned but not cited (13)

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Articles - 4ake mentioned but not cited (148)



Reviews citing this publication (8)

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  7. Seeing the forest for the trees: fluorescence studies of single enzymes in the context of ensemble experiments. Tan YW, Yang H. Phys Chem Chem Phys 13 1709-1721 (2011)
  8. Anisotropic nuclear spin interactions for the morphology analysis of proteins in solution by NMR spectroscopy. Tate S. Anal Sci 24 39-50 (2008)

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