4NTM

QueD soaked with sepiapterin (selenomethionine substituted protein)

4NTM の概要

• エントリーDOI: 10.2210/pdb4ntm/pdb
• 関連するPDBエントリー: 4NTK 4NTN
• 分子名称: 6-carboxy-5,6,7,8-tetrahydropterin synthase, ZINC ION, (6R)-2-amino-4-oxo-3,4,5,6,7,8-hexahydropteridine-6-carboxylic acid, ... (4 entities in total)
• 機能のキーワード: t-fold, 6-ptps, queuosine biosynthesis enzyme, sepiapterin, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 85542.29

構造登録者

Bandarian, V.,Miles, Z.D.,Roberts, S.A. (登録日: 2013-12-02, 公開日: 2014-07-16, 最終更新日: 2024-11-06)

主引用文献

Miles, Z.D.,Roberts, S.A.,McCarty, R.M.,Bandarian, V.
Biochemical and Structural Studies of 6-Carboxy-5,6,7,8-tetrahydropterin Synthase Reveal the Molecular Basis of Catalytic Promiscuity within the Tunnel-fold Superfamily.
J.Biol.Chem., 289:23641-23652, 2014

PubMed Abstract: 6-Pyruvoyltetrahydropterin synthase (PTPS) homologs in both mammals and bacteria catalyze distinct reactions using the same 7,8-dihydroneopterin triphosphate substrate. The mammalian enzyme converts 7,8-dihydroneopterin triphosphate to 6-pyruvoyltetrahydropterin, whereas the bacterial enzyme catalyzes the formation of 6-carboxy-5,6,7,8-tetrahydropterin. To understand the basis for the differential activities we determined the crystal structure of a bacterial PTPS homolog in the presence and absence of various ligands. Comparison to mammalian structures revealed that although the active sites are nearly structurally identical, the bacterial enzyme houses a His/Asp dyad that is absent from the mammalian protein. Steady state and time-resolved kinetic analysis of the reaction catalyzed by the bacterial homolog revealed that these residues are responsible for the catalytic divergence. This study demonstrates how small variations in the active site can lead to the emergence of new functions in existing protein folds.

PubMed: 24990950
DOI: 10.1074/jbc.M114.555680

実験手法

X-RAY DIFFRACTION (2.05 Å)