7wrm

The malate-bound dimer of chemoreceptor MCP2201 ligand binding domain

spinqualitylabelsall models 7wrm, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7wrm is a 2 chain structure with sequence from Comamonas testosteroni CNB-2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: LMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Motile bacteria navigate toward favorable conditions and away from unfavorable environments using chemotaxis. Mechanisms of sensing attractants are well understood; however, molecular aspects of how bacteria sense repellents have not been established. Here, we identified malate as a repellent recognized by the MCP2201 chemoreceptor in a bacterium Comamonas testosteroni and showed that it binds to the same site as an attractant citrate. Binding determinants for a repellent and an attractant had only minor differences, and a single amino acid substitution in the binding site inverted the response to malate from a repellent to an attractant. We found that malate and citrate affect the oligomerization state of the ligand-binding domain in opposing way. We also observed opposing effects of repellent and attractant binding on the orientation of an alpha helix connecting the sensory domain to the transmembrane helix. We propose a model to illustrate how positive and negative signals might be generated. Attractant and repellent induce opposing changes in the four-helix bundle ligand-binding domain of a bacterial chemoreceptor.,Guo L, Wang YH, Cui R, Huang Z, Hong Y, Qian JW, Ni B, Xu AM, Jiang CY, Zhulin IB, Liu SJ, Li DF PLoS Biol. 2023 Dec 11;21(12):e3002429. doi: 10.1371/journal.pbio.3002429. , eCollection 2023 Dec. PMID:38079456 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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