5F9Q

Crystal structure of the extracellular domain of noncanonic ABC-type transporter YknZ from Gram-positive bacteria

5F9Q の概要

• エントリーDOI: 10.2210/pdb5f9q/pdb
• 分子名称: Macrolide export ATP-binding/permease protein YknZ (2 entities in total)
• 機能のキーワード: bacillus amyloliquefaciens, sdp transporter yknwxyz, respective permease yknz, membrane protein
• 由来する生物種: Bacillus amyloliquefaciens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22082.58

構造登録者

Xu, Y.,Guo, J.,Jiang, R.,Jin, X.,Fan, S.,Quan, C.S.,Ha, N.C. (登録日: 2015-12-10, 公開日: 2016-02-03, 最終更新日: 2024-10-23)

主引用文献

Xu, Y.,Guo, J.,Wang, L.,Jiang, R.,Jin, X.,Liu, J.,Fan, S.,Quan, C.S.,Ha, N.C.
The Crystal Structure of the YknZ Extracellular Domain of ABC Transporter YknWXYZ from Bacillus amyloliquefaciens.
Plos One, 11:e0155846-e0155846, 2016

PubMed Abstract: Bacillus possesses the peptide toxin Sporulation-Delaying Protein (SDP), which can kill cells within a biofilm to support continued growth, thereby delaying the onset of biofilm sporulation. The four-component transporter YknWXYZ acts as a major SDP efflux pump to protect cells against the endogenous SDP toxin, for which YknYZ is a non-canonical ATP-binding cassette (ABC)-type transporter. YknYZ consists of the following two components: (1) an individual protein (YknY) and (2) a respective permease (YknZ). To date, the crystal structure, molecular function, and mechanism of action of the integral membrane protein YknZ remain to be elucidated. In this study, to characterize the structural and biochemical roles of YknZ in the functional assembly of YknWXYZ, we predicted and overexpressed the YknZ extracellular domain. We determined the crystal structure of B. amyloliquefaciens YknZ at a resolution of 2.0 Å. The structure revealed that the YknZ extracellular region exhibits significant structural similarity with the MacB periplasmic domain, which is a non-canonical ABC-type transporter in the tripartite macrolide-specific efflux pump in Gram-negative bacteria. We also found that the YknZ extracellular domain can directly bind to an extracellular component of YknX. This structural and biochemical study provides insights into the assembly of YknWXYZ, which may be relevant to understanding cannibalistic peptide toxin resistance in Bacillus and controlling bacterial growth.

PubMed: 27243566
DOI: 10.1371/journal.pone.0155846

実験手法

X-RAY DIFFRACTION (2.044 Å)