4NC9

Crystal structure of phosphatidyl mannosyltransferase PimA

4NC9 の概要

• エントリーDOI: 10.2210/pdb4nc9/pdb
• 関連するPDBエントリー: 4N9W
• 分子名称: GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase (2 entities in total)
• 機能のキーワード: gt-b, transferase
• 由来する生物種: Mycobacterium smegmatis
• 細胞内の位置: Cell membrane ; Single-pass membrane protein : A0QWG6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166164.75

構造登録者

Giganti, D.,Albesa-Jove, D.,Bellinzoni, M.,Guerin, M.E.,Alzari, P.M. (登録日: 2013-10-24, 公開日: 2014-11-12, 最終更新日: 2023-09-20)

主引用文献

Giganti, D.,Albesa-Jove, D.,Urresti, S.,Rodrigo-Unzueta, A.,Martinez, M.A.,Comino, N.,Barilone, N.,Bellinzoni, M.,Chenal, A.,Guerin, M.E.,Alzari, P.M.
Secondary structure reshuffling modulates glycosyltransferase function at the membrane.
Nat.Chem.Biol., 11:16-18, 2015

PubMed Abstract: Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand-to-α-helix and α-helix-to-β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.

PubMed: 25402770
DOI: 10.1038/nchembio.1694

実験手法

X-RAY DIFFRACTION (3.192 Å)