6HRC

Outward-facing PglK with ATPgammaS bound

6HRC の概要

• エントリーDOI: 10.2210/pdb6hrc/pdb
• 関連するPDBエントリー: 5C73 5C76 5C78 5NBD
• 分子名称: WlaB protein, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: abc transporter, transport protein
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 260380.08

構造登録者

Perez, C.,Locher, K.P. (登録日: 2018-09-26, 公開日: 2019-03-06, 最終更新日: 2024-01-24)

主引用文献

Perez, C.,Mehdipour, A.R.,Hummer, G.,Locher, K.P.
Structure of Outward-Facing PglK and Molecular Dynamics of Lipid-Linked Oligosaccharide Recognition and Translocation.
Structure, 27:669-678.e5, 2019

PubMed Abstract: PglK is a lipid-linked oligosaccharide (LLO) flippase essential for asparagine-linked protein glycosylation in Campylobacter jejuni. Previously we have proposed a non-alternating-access LLO translocation mechanism, where postulated outward-facing states play a primary role. To investigate this unusual mechanistic proposal, we have determined a high-resolution structure of PglK that displays an outward semi-occluded state with the two nucleotide binding domains forming an asymmetric closed dimer with two bound ATPγS molecules. Based on this structure, we performed extensive molecular dynamics simulations to investigate LLO recognition and flipping. Our results suggest that PglK may employ a "substrate-hunting" mechanism to locally increase the LLO concentration and facilitate its jump into the translocation pathway, for which sugars from the LLO head group are essential. We further conclude that the release of LLO to the outside occurs before ATP hydrolysis and is followed by the closing of the periplasmic cavity of PglK.

PubMed: 30799077
DOI: 10.1016/j.str.2019.01.013

実験手法

X-RAY DIFFRACTION (3.3 Å)