2YOC

Crystal structure of PulA from Klebsiella oxytoca

2YOC の概要

• エントリーDOI: 10.2210/pdb2yoc/pdb
• 分子名称: PULLULANASE, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, glycosyl hydrolase, type 2 secretion systems
• 由来する生物種: KLEBSIELLA OXYTOCA
• 細胞内の位置: Cell membrane ; Lipid-anchor : P07206
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 238215.33

構造登録者

Francetic, O.,Mechaly, A.E.,Tello-Manigne, D.,Buschiazzo, A.,Bernarde, C.,Nadeau, N.,Pugsley, A.P.,Alzari, P.M. (登録日: 2012-10-23, 公開日: 2013-11-06, 最終更新日: 2024-11-06)

主引用文献

East, A.,Mechaly, A.E.,Huysmans, G.H.M.,Bernarde, C.,Tello-Manigne, D.,Nadeau, N.,Pugsley, A.P.,Buschiazzo, A.,Alzari, P.M.,Bond, P.J.,Francetic, O.
Structural Basis of Pullulanase Membrane Binding and Secretion Revealed by X-Ray Crystallography, Molecular Dynamics and Biochemical Analysis
Structure, 24:92-, 2016

PubMed Abstract: The Klebsiella lipoprotein pullulanase (PulA) is exported to the periplasm, triacylated, and anchored via lipids in the inner membrane (IM) prior to its transport to the bacterial surface through a type II secretion system (T2SS). X-Ray crystallography and atomistic molecular dynamics (MD) simulations of PulA in a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) model membrane provided an unprecedented molecular view of an N-terminal unstructured tether and the IM lipoprotein retention signal, and revealed novel interactions with the IM via N-terminal immunoglobulin-like domains in PulA. An efficiently secreted nonacylated variant (PulANA) showed similar peripheral membrane association during MD simulations, consistent with the binding of purified PulANA to liposomes. Remarkably, combined X-ray, MD, and functional studies identified a novel subdomain, Ins, inserted in the α-amylase domain, which is required for PulA secretion. Available data support a model in which PulA binding to the IM promotes interactions with the T2SS, possibly via the Ins subdomain.

PubMed: 26688215
DOI: 10.1016/J.STR.2015.10.023

実験手法

X-RAY DIFFRACTION (2.88 Å)