5W95

Mtb Rv3802c with PEG bound

5W95 の概要

• エントリーDOI: 10.2210/pdb5w95/pdb
• 分子名称: Conserved membrane protein of uncharacterised function, PENTAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: peg, complex, hydrolase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61552.82

構造登録者

Goins, C.M.,Schreidah, C.M.,Ronning, D.R. (登録日: 2017-06-22, 公開日: 2017-12-27, 最終更新日: 2024-11-06)

主引用文献

Goins, C.M.,Schreidah, C.M.,Dajnowicz, S.,Ronning, D.R.
Structural basis for lipid binding and mechanism of the Mycobacterium tuberculosis Rv3802 phospholipase.
J. Biol. Chem., 293:1363-1372, 2018

PubMed Abstract: The gene encodes an essential enzyme with thioesterase and phospholipase A activity. Overexpression of Rv3802 orthologs in and increases mycolate content and decreases glycerophospholipids. Although a role in modulating the lipid composition of the unique mycomembrane has been proposed, the true biological function of Rv3802 remains uncertain. In this study, we present the first Rv3802 X-ray crystal structure, solved to 1.7 Å resolution. On the basis of the binding of PEG molecules to Rv3802, we identified its lipid-binding site and the structural basis for phosphatidyl-based substrate binding and phospholipase A activity. We found that movement of the α8-helix affords lipid binding and is required for catalytic turnover through covalent tethering. We gained insights into the mechanism of acyl hydrolysis by observing differing arrangements of PEG and water molecules within the active site. This study provides structural insights into biological function and facilitates future structure-based drug design toward Rv3802.

PubMed: 29247008
DOI: 10.1074/jbc.RA117.000240

実験手法

X-RAY DIFFRACTION (1.723 Å)