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Structural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in

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Two‐component and phosphorelay signal‐transduction proteins are crucial for bacterial cell‐cycle regulation in Caulobacter crescentus. ChpT is an essential histidine phosphotransferase that controls the activity of the master cell‐cycle regulator CtrA by phosphorylation. Here, the 2.2 Å resolution crystal structure of ChpT is reported. ChpT is a homodimer and adopts the domain architecture of the intracellular part of class I histidine kinases. Each subunit consists of two distinct domains: an N‐terminal helical hairpin domain and a C‐terminal α/β domain. The two N‐terminal domains are adjacent within the dimer, forming a four‐helix bundle. The ChpT C‐terminal domain adopts an atypical Bergerat ATP‐binding fold.
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Document Type: Research Article

Affiliations: Interdisciplinary Research Institute, USR 3078 CNRS – Université Lille Nord de France, Parc CNRS de la Haute Borne, 50 Avenue de Halley, 59658 Villeneuve d'Ascq, France

Publication date: September 1, 2012

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