1S3H

Propionibacterium shermanii transcarboxylase 5S subunit A59T

1S3H の概要

• エントリーDOI: 10.2210/pdb1s3h/pdb
• 関連するPDBエントリー: 1RQB 1RQE 1RQH 1RR2 1S27
• 分子名称: transcarboxylase 5S subunit, COBALT (II) ION (3 entities in total)
• 機能のキーワード: tim-barrel, carbamylated lysine, transcarboxylase, cobalt, transferase
• 由来する生物種: Propionibacterium freudenreichii subsp. shermanii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59741.43

構造登録者

Hall, P.R.,Zheng, R.,Antony, L.,Pusztai-Carey, M.,Carey, P.R.,Yee, V.C. (登録日: 2004-01-13, 公開日: 2004-09-07, 最終更新日: 2023-11-15)

主引用文献

Hall, P.R.,Zheng, R.,Antony, L.,Pusztai-Carey, M.,Carey, P.R.,Yee, V.C.
Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.
Embo J., 23:3621-3631, 2004

PubMed Abstract: Transcarboxylase is a 1.2 million Dalton (Da) multienzyme complex from Propionibacterium shermanii that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate to yield propionyl-CoA and oxaloacetate. Crystal structures of the 5S metalloenzyme subunit, which catalyzes the second carboxylation reaction, have been solved in free form and bound to its substrate pyruvate, product oxaloacetate, or inhibitor 2-ketobutyrate. The structure reveals a dimer of beta(8)alpha(8) barrels with an active site cobalt ion coordinated by a carbamylated lysine, except in the oxaloacetate complex in which the product's carboxylate group serves as a ligand instead. 5S and human pyruvate carboxylase (PC), an enzyme crucial to gluconeogenesis, catalyze similar reactions. A 5S-based homology model of the PC carboxyltransferase domain indicates a conserved mechanism and explains the molecular basis of mutations in lactic acidemia. PC disease mutations reproduced in 5S result in a similar decrease in carboxyltransferase activity and crystal structures with altered active sites.

PubMed: 15329673
DOI: 10.1038/sj.emboj.7600373

実験手法

X-RAY DIFFRACTION (2.5 Å)