1EUD

CRYSTAL STRUCTURE OF PHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE

1EUD の概要

• エントリーDOI: 10.2210/pdb1eud/pdb
• 関連するPDBエントリー: 1CQI 1CQJ 1EUC 2SCU
• 分子名称: SUCCINYL-COA SYNTHETASE, ALPHA CHAIN, SUCCINYL-COA SYNTHETASE, BETA CHAIN, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ligase, gtp-specific, phosphonohistidine
• 由来する生物種: Sus scrofa (pig); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75917.93

構造登録者

Fraser, M.E.,James, M.N.G.,Bridger, W.A.,Wolodko, W.T. (登録日: 2000-04-14, 公開日: 2000-07-27, 最終更新日: 2021-11-03)

主引用文献

Fraser, M.E.,James, M.N.,Bridger, W.A.,Wolodko, W.T.
Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase.
J.Mol.Biol., 299:1325-1339, 2000

PubMed Abstract: Succinyl-CoA synthetase (SCS) catalyzes the reversible phosphorylation/dephosphorylation reaction:¿¿¿rm succinyl ¿hbox ¿-¿CoA+NDP+P_i¿leftrightarrow succinate+CoA+NTP¿¿where N denotes adenosine or guanosine. In the course of the reaction, an essential histidine residue is transiently phosphorylated. We have crystallized and solved the structure of the GTP-specific isoform of SCS from pig heart (EC 6.2.1.4) in both the dephosphorylated and phosphorylated forms. The structures were refined to 2.1 A resolution. In the dephosphorylated structure, the enzyme is stabilized via coordination of a phosphate ion by the active-site histidine residue and the two "power" helices, one contributed by each subunit of the alphabeta-dimer. Small changes in the conformations of residues at the amino terminus of the power helix contributed by the alpha-subunit allow the enzyme to accommodate either the covalently bound phosphoryl group or the free phosphate ion. Structural comparisons are made between the active sites in these two forms of the enzyme, both of which can occur along the catalytic path. Comparisons are also made with the structure of Escherichia coli SCS. The domain that has been shown to bind ADP in E. coli SCS is more open in the pig heart, GTP-specific SCS structure.

PubMed: 10873456
DOI: 10.1006/jmbi.2000.3807

実験手法

X-RAY DIFFRACTION (2.1 Å)