4P29

Crystal structure of the LpoA N-terminal domain from Haemophilus influenzae

4P29 の概要

• エントリーDOI: 10.2210/pdb4p29/pdb
• 関連するPDBエントリー: 2MHK 3CKM
• 分子名称: LpoA, SULFATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: peptidoglycan synthesis, tpr-like, outer membrane lipoprotein, protein binding
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53306.19

構造登録者

Vijayalakshmi, J.,Saper, M.A. (登録日: 2014-03-02, 公開日: 2015-03-04, 最終更新日: 2024-10-16)

主引用文献

Sathiyamoorthy, K.,Vijayalakshmi, J.,Tirupati, B.,Fan, L.,Saper, M.A.
Structural analyses of theHaemophilus influenzaepeptidoglycan synthase activator LpoA suggest multiple conformations in solution.
J.Biol.Chem., 292:17626-17642, 2017

PubMed Abstract: In many Gram-negative bacteria, the peptidoglycan synthase PBP1A requires the outer membrane lipoprotein LpoA for constructing a functional peptidoglycan required for bacterial viability. Previously, we have shown that the C-terminal domain of LpoA (LpoA) has a highly conserved, putative substrate-binding cleft between two α/β lobes. Here, we report a 2.0 Å resolution crystal structure of the LpoA N-terminal domain. Two subdomains contain tetratricopeptide-like motifs that form a concave groove, but their relative orientation differs by ∼45° from that observed in an NMR structure of the LpoA N domain. We also determined three 2.0-2.8 Å resolution crystal structures containing four independent full-length LpoA molecules. In contrast to an elongated model previously suggested for LpoA, each LpoA formed a U-shaped structure with a different C-domain orientation. This resulted from both N-domain twisting and rotation of the C domain (up to 30°) at the end of the relatively immobile interdomain linker. Moreover, a previously predicted hinge between the lobes of the LpoA C domain exhibited variations of up to 12°. Small-angle X-ray scattering data revealed excellent agreement with a model calculated by normal mode analysis from one of the full-length LpoA molecules but even better agreement with an ensemble of this molecule and two of the partially extended normal mode analysis-predicted models. The different LpoA structures helped explain how an outer membrane-anchored LpoA can either withdraw from or extend toward the inner membrane-bound PBP1A through peptidoglycan gaps and hence regulate the synthesis of peptidoglycan necessary for bacterial viability.

PubMed: 28887305
DOI: 10.1074/jbc.M117.804997

実験手法

X-RAY DIFFRACTION (1.95006475032 Å)