7MIE

Crystal structure of the Borreliella burgdorferi PlzA protein in complex with c-di-GMP

7MIE の概要

• エントリーDOI: 10.2210/pdb7mie/pdb
• 分子名称: PlzA, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: tick-borne pathogens, borreliella burgdorferi, pilz domain, c-di-gmp-binding receptor signaling, signaling protein
• 由来する生物種: Borrelia burgdorferi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33587.14

構造登録者

Davies, C.,Singh, A. (登録日: 2021-04-16, 公開日: 2021-06-30, 最終更新日: 2024-05-22)

主引用文献

Singh, A.,Izac, J.R.,Schuler, E.J.A.,Patel, D.T.,Davies, C.,Marconi, R.T.
High-resolution crystal structure of the Borreliella burgdorferi PlzA protein in complex with c-di-GMP: new insights into the interaction of c-di-GMP with the novel xPilZ domain.
Pathog Dis, 79:-, 2021

PubMed Abstract: In the tick-borne pathogens, Borreliella burgdorferi and Borrelia hermsii, c-di-GMP is produced by a single diguanylate cyclase (Rrp1). In these pathogens, the Plz proteins (PlzA, B and C) are the only c-di-GMP receptors identified to date and PlzA is the sole c-di-GMP receptor found in all Borreliella isolates. Bioinformatic analyses suggest that PlzA has a unique PilZN3-PilZ architecture with the relatively uncommon xPilZ domain. Here, we present the crystal structure of PlzA in complex with c-di-GMP (1.6 Å resolution). This is the first structure of a xPilz domain in complex with c-di-GMP to be determined. PlzA has a two-domain structure, where each domain comprises topologically equivalent PilZ domains with minimal sequence identity but remarkable structural similarity. The c-di-GMP binding site is formed by the linker connecting the two domains. While the structure of apo PlzA could not be determined, previous fluorescence resonance energy transfer data suggest that apo and holo forms of the protein are structurally distinct. The information obtained from this study will facilitate ongoing efforts to identify the molecular mechanisms of PlzA-mediated regulation in ticks and mammals.

PubMed: 34117751
DOI: 10.1093/femspd/ftab030

実験手法

X-RAY DIFFRACTION (1.6 Å)