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ATP forms a stable complex with the essential histidine kinase WalK (YycG) domain

Authors
Journal
Acta Crystallographica Section D Biological Crystallography
0907-4449
Publisher
International Union of Crystallography
Publication Date
Volume
68
Issue
7
Identifiers
DOI: 10.1107/s090744491201373x
Keywords
  • Research Papers

Abstract

The histidine WalK (YycG) plays a crucial role in coordinating murein synthesis with cell division and the crystal structure of its ATP binding domain has been determined. Interestingly the bound ATP was not hydrolyzed during crystallization and remains intact in the crystal lattice.

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