3C9T

AaThiL complexed with AMPPCP and TMP

3C9T の概要

• エントリーDOI: 10.2210/pdb3c9t/pdb
• 関連するPDBエントリー: 3C9R 3C9S 3C9U
• 分子名称: Thiamine monophosphate kinase, MAGNESIUM ION, THIAMIN PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: beta barrel, alpha-beta structure, kinase, transferase
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78883.99

構造登録者

McCulloch, K.M.,Kinsland, C.,Begley, T.P.,Ealick, S.E. (登録日: 2008-02-18, 公開日: 2008-03-18, 最終更新日: 2024-11-20)

主引用文献

McCulloch, K.M.,Kinsland, C.,Begley, T.P.,Ealick, S.E.
Structural studies of thiamin monophosphate kinase in complex with substrates and products.
Biochemistry, 47:3810-3821, 2008

PubMed Abstract: Thiamin monophosphate kinase (ThiL) catalyzes the ATP-dependent phosphorylation of thiamin monophosphate (TMP) to form thiamin pyrophosphate (TPP), the active form of vitamin B 1. ThiL is a member of a small ATP binding superfamily that also includes the purine biosynthetic enzymes, PurM and PurL, NiFe hydrogenase maturation protein, HypE, and selenophosphate synthase, SelD. The latter four enzymes are believed to utilize phosphorylated intermediates during catalysis. To understand the mechanism of ThiL and its relationship to the other superfamily members, we determined the structure of Aquifex aeolicus ThiL (AaThiL) with nonhydrolyzable AMP-PCP and TMP, and also with the products of the reaction, ADP and TPP. The results suggest that AaThiL utilizes a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate. The structure of ThiL is compared to those of PurM, PurL, and HypE, and the ATP binding site is compared to that of PurL, for which nucleotide complexes are available.

PubMed: 18311927
DOI: 10.1021/bi800041h

実験手法

X-RAY DIFFRACTION (2.6 Å)