6M5O

Co-crystal structure of human serine hydroxymethyltransferase 2 in complex with Pyridoxal 5'-phosphate (PLP) and glycodeoxycholic acid

6M5O の概要

• エントリーDOI: 10.2210/pdb6m5o/pdb
• 分子名称: Serine hydroxymethyltransferase, mitochondrial, (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID, GLYCINE, ... (4 entities in total)
• 機能のキーワード: inhibitor, complex, transferase
• 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: 113620.89

構造登録者

Ota, T.,Senoo, A.,Ito, S.,Ueno, G.,Nagatoishi, S.,Tsumoto, K.,Sando, S. (登録日: 2020-03-11, 公開日: 2021-01-20, 最終更新日: 2023-11-29)

主引用文献

Ota, T.,Senoo, A.,Shirakawa, M.,Nonaka, H.,Saito, Y.,Ito, S.,Ueno, G.,Nagatoishi, S.,Tsumoto, K.,Sando, S.
Structural basis for selective inhibition of human serine hydroxymethyltransferase by secondary bile acid conjugate.
Iscience, 24:102036-102036, 2021

PubMed Abstract: Bile acids are metabolites of cholesterol that facilitate lipid digestion and absorption in the small bowel. Bile acids work as agonists of receptors to regulate their own metabolism. Bile acids also regulate other biological systems such as sugar metabolism, intestinal multidrug resistance, and adaptive immunity. However, numerous physiological roles of bile acids remain undetermined. In this study, we solved the crystal structure of human serine hydroxymethyltransferase (hSHMT) in complex with an endogenous secondary bile acid glycine conjugate. The specific interaction between hSHMT and the ligand was demonstrated using mutational analyses, biophysical measurements, and structure-activity relationship studies, suggesting that secondary bile acid conjugates may act as modulators of SHMT activity.

PubMed: 33521601
DOI: 10.1016/j.isci.2021.102036

実験手法

X-RAY DIFFRACTION (2.30000663987 Å)