Structure and signaling mechanism of <i>Helicobacter pylori</i> transducer-like protein D.

ABSTRACT: Chemoreceptors, or methyl-accepting chemotaxis proteins (MCPs), are ancient and widespread prokaryotic sensors that direct taxis in response to stimuli and are attractive targets for therapeutic control of bacteria^1-4. Decades of study have yielded substantial mechanistic insight into chemoreceptor function, but the absence of high-resolution full-length structures containing ligand-binding domains (LBD) has limited understanding of how effector sensing is structurally coupled to long-range signal transduction. Here, we present the intact structure of the chemoreceptor transducer-like protein D (TlpD) from the gastric pathogen Helicobacter pylori, in complex with its ligand Zn²⁺, determined by X-ray crystallography in two crystal forms at 2.4-3.0 Å. Three diffe

SUBMITTER: Franco K 

PROVIDER: S-EPMC12871147 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature