3H6D

Structure of the mycobacterium tuberculosis DUTPase D28N mutant

3H6D の概要

• エントリーDOI: 10.2210/pdb3h6d/pdb
• 分子名称: Deoxyuridine 5'-triphosphate nucleotidohydrolase, MAGNESIUM ION, 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: jelly-roll, hydrolase, nucleotide metabolism
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18727.08

構造登録者

Leveles, I.,Harmat, V.,Nagy, G.,Takacs, E.,Lopata, A.,Toth, J.,Vertessy, B.G. (登録日: 2009-04-23, 公開日: 2009-11-24, 最終更新日: 2023-09-06)

主引用文献

Takacs, E.,Nagy, G.,Leveles, I.,Harmat, V.,Lopata, A.,Toth, J.,Vertessy, B.G.
Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases.
Febs Lett., 584:3047-3054, 2010

PubMed Abstract: dUTP pyrophosphatases (dUTPases) are essential for genome integrity. Recent results allowed characterization of the role of conserved residues. Here we analyzed the Asp/Asn mutation within conserved Motif I of human and mycobacterial dUTPases, wherein the Asp residue was previously implicated in Mg(2+)-coordination. Our results on transient/steady-state kinetics, ligand binding and a 1.80 A resolution structure of the mutant mycobacterial enzyme, in comparison with wild type and C-terminally truncated structures, argue that this residue has a major role in providing intra- and intersubunit contacts, but is not essential for Mg(2+) accommodation. We conclude that in addition to the role of conserved motifs in substrate accommodation, direct subunit interaction between protein atoms of active site residues from different conserved motifs are crucial for enzyme function.

PubMed: 20493855
DOI: 10.1016/j.febslet.2010.05.018

実験手法

X-RAY DIFFRACTION (1.8 Å)