4BGF

The 3D-structure of arylamine-N-acetyltransferase from M. tuberculosis

4BGF の概要

• エントリーDOI: 10.2210/pdb4bgf/pdb
• 分子名称: ARYLAMINE N-ACETYLTRANSFERASE NAT (2 entities in total)
• 機能のキーワード: transferase, drug design, cross-seeding, micro-seeding, microseed matrix screen
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 248504.95

構造登録者

Abuhammad, A.,Lowe, E.D.,McDonough, M.A.,Shaw Stewart, P.D.,Kolek, S.A.,Sim, E.,Garman, E.F. (登録日: 2013-03-26, 公開日: 2013-07-24, 最終更新日: 2023-12-20)

主引用文献

Abuhammad, A.,Lowe, E.D.,McDonough, M.A.,Shaw Stewart, P.D.,Kolek, S.A.,Sim, E.,Garman, E.F.
Structure of arylamine N-acetyltransferase from Mycobacterium tuberculosis determined by cross-seeding with the homologous protein from M. marinum: triumph over adversity.
Acta Crystallogr. D Biol. Crystallogr., 69:1433-1446, 2013

PubMed Abstract: Arylamine N-acetyltransferase from Mycobacterium tuberculosis (TBNAT) plays an important role in the intracellular survival of the microorganism inside macrophages. Medicinal chemistry efforts to optimize inhibitors of the TBNAT enzyme have been hampered by the lack of a three-dimensional structure of the enzyme. In this paper, the first structure of TBNAT, determined using a lone crystal produced using cross-seeding with the homologous protein from M. marinum, is reported. Despite the similarity between the two enzymes (74% sequence identity), they show distinct physical and biochemical characteristics. The structure elegantly reveals the characteristic features of the protein surface as well as details of the active site of TBNAT relevant to drug-discovery efforts. The crystallographic analysis of the diffraction data presented many challenges, since the crystal was twinned and the habit possessed pseudo-translational symmetry.

PubMed: 23897467
DOI: 10.1107/S0907444913015126

実験手法

X-RAY DIFFRACTION (2.097 Å)