2NT8

ATP bound at the active site of a PduO type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri

2NT8 の概要

• エントリーDOI: 10.2210/pdb2nt8/pdb
• 分子名称: Cobalamin adenosyltransferase, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: atp binding, transferase
• 由来する生物種: Lactobacillus reuteri
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26447.64

構造登録者

St-Maurice, M.,Mera, P.E.,Taranto, M.P.,Sesma, F.,Escalante-Semerena, J.C.,Rayment, I. (登録日: 2006-11-07, 公開日: 2006-11-21, 最終更新日: 2023-08-30)

主引用文献

St Maurice, M.,Mera, P.E.,Taranto, M.P.,Sesma, F.,Escalante-Semerena, J.C.,Rayment, I.
Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri.
J.Biol.Chem., 282:2596-2605, 2007

PubMed Abstract: The three-dimensional crystal structure of the PduO-type corrinoid adenosyltransferase from Lactobacillus reuteri (LrPduO) has been solved to 1.68-A resolution. The functional assignment of LrPduO as a corrinoid adenosyltransferase was confirmed by in vivo and in vitro evidence. The enzyme has an apparent Km(ATP) of 2.2 microM and Km(Cobalamin) of 0.13 microM and a kcat of 0.025 s(-1). Co-crystallization of the enzyme with Mg-ATP resulted in well-defined electron density for an N-terminal loop that had been disordered in other PduO-type enzyme structures. This newly defined N-terminal loop makes up the lower portion of the enzyme active site with the other half being contributed from an adjacent subunit. These results provide the first detailed description of the enzyme active site for a PduO-type adenosyltransferase and identify a unique ATP binding motif at the protein N terminus. The molecular architecture at the active site offers valuable new insight into the role of various residues responsible for the human disease methylmalonic aciduria.

PubMed: 17121823
DOI: 10.1074/jbc.M609557200

実験手法

X-RAY DIFFRACTION (1.68 Å)