5IIP

Staphylococcus aureus OpuCA

5IIP の概要

• エントリーDOI: 10.2210/pdb5iip/pdb
• 分子名称: Glycine betaine/carnitine/choline ABC transporter%2C ATP-binding protein%2C putative (2 entities in total)
• 機能のキーワード: cbs domain, osmoprotection, c-di-amp, transport protein
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 87489.58

構造登録者

Tosi, T.,Campeotto, I.,Freemont, P.S.,Grundling, A. (登録日: 2016-03-01, 公開日: 2016-08-24, 最終更新日: 2024-01-10)

主引用文献

Schulte, L.E.,Schuster, C.F.,Tosi, T.,Campeotto, I.,Corrigan, R.M.,Freemont, P.S.,Grundling, A.
The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus.
Sci.Signal., 9:441-, 2016

PubMed Abstract: Staphylococcus aureus is an important opportunistic human pathogen that is highly resistant to osmotic stresses. To survive an increase in osmolarity, bacteria immediately take up potassium ions and small organic compounds known as compatible solutes. The second messenger cyclic diadenosine monophosphate (c-di-AMP) reduces the ability of bacteria to withstand osmotic stress by binding to and inhibiting several proteins that promote potassium uptake. We identified OpuCA, the adenosine triphosphatase (ATPase) component of an uptake system for the compatible solute carnitine, as a c-di-AMP target protein in S aureus and found that the LAC*ΔgdpP strain of S aureus, which overproduces c-di-AMP, showed reduced carnitine uptake. The paired cystathionine-β-synthase (CBS) domains of OpuCA bound to c-di-AMP, and a crystal structure revealed a putative binding pocket for c-di-AMP in the cleft between the two CBS domains. Thus, c-di-AMP inhibits osmoprotection through multiple mechanisms.

PubMed: 27531650
DOI: 10.1126/scisignal.aaf7279

実験手法

X-RAY DIFFRACTION (2.5 Å)