7Y63

ApoSIDT2-pH7.4

7Y63 の概要

• エントリーDOI: 10.2210/pdb7y63/pdb
• EMDBエントリー: 33632
• 分子名称: SID1 transmembrane family member 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (4 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 192235.55

構造登録者

Gong, D.S. (登録日: 2022-06-18, 公開日: 2023-06-21, 最終更新日: 2024-11-20)

主引用文献

Qian, D.,Cong, Y.,Wang, R.,Chen, Q.,Yan, C.,Gong, D.S.
Structural insight into the human SID1 transmembrane family member 2 reveals its lipid hydrolytic activity.
Nat Commun, 14:3568-3568, 2023

PubMed Abstract: The systemic RNAi-defective (SID) transmembrane family member 2 (SIDT2) is a putative nucleic acid channel or transporter that plays essential roles in nucleic acid transport and lipid metabolism. Here, we report the cryo-electron microscopy (EM) structures of human SIDT2, which forms a tightly packed dimer with extensive interactions mediated by two previously uncharacterized extracellular/luminal β-strand-rich domains and the unique transmembrane domain (TMD). The TMD of each SIDT2 protomer contains eleven transmembrane helices (TMs), and no discernible nucleic acid conduction pathway has been identified within the TMD, suggesting that it may act as a transporter. Intriguingly, TM3-6 and TM9-11 form a large cavity with a putative catalytic zinc atom coordinated by three conserved histidine residues and one aspartate residue lying approximately 6 Å from the extracellular/luminal surface of the membrane. Notably, SIDT2 can hydrolyze C18 ceramide into sphingosine and fatty acid with a slow rate. The information presented advances the understanding of the structure-function relationships in the SID1 family proteins.

PubMed: 37322007
DOI: 10.1038/s41467-023-39335-2

実験手法

ELECTRON MICROSCOPY (3.16 Å)