4QFW

Crystal structure of acyl-CoA thioesterase tesB from Yersinia pestis

「4GWH」から置き換えられました

4QFW の概要

• エントリーDOI: 10.2210/pdb4qfw/pdb
• 分子名称: Acyl-CoA thioesterase II (2 entities in total)
• 機能のキーワード: double-hotdog, 4hbt-like, thioesterase, acyl-coa thioesterase, hydrolase
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 130811.68

構造登録者

Swarbrick, C.M.D.,Forwood, J.K. (登録日: 2014-05-21, 公開日: 2014-06-04, 最終更新日: 2023-09-20)

主引用文献

Swarbrick, C.M.,Patterson, E.I.,Forwood, J.K.
Crystallization of the acyl-CoA thioesterase TesB from Yersinia pestis.
Acta Crystallogr.,Sect.F, 69:188-190, 2013

PubMed Abstract: Yersinia pestis is a highly virulent human pathogen and is the causative agent of bubonic plague. Spread through the bite of infected fleas, plague epidemics have marked important events in history, including the Justinian plague (6th century), the Black Death (14th century) which decimated nearly one quarter of the European population, and more recently the Orientalis plague (1894). To date, deaths are still being reported and, without treatment, the disease kills most people within 4 days. One of the thioesterases from Y. pestis, TesB, is a broad-range acyl-CoA thioesterase and is highly conserved within prokaryotes and throughout evolution, sharing sequence similarity with the HIV Nef binding protein ACOT8. Here the expression, purification, crystallization and diffraction of TesB are reported. TesB has been recombinantly expressed and crystallized using the vapour-diffusion hanging-drop technique at pH 7.0 and 290 K. After optimization, crystals diffracted to 2.0 Å resolution at the Australian Synchrotron and belong to the space group P12(1)1 (a = 73.55, b = 170.82, c = 101.98 Å), with eight molecules likely to be present in the asymmetric unit.

PubMed: 23385765
DOI: 10.1107/S1744309113001267

実験手法

X-RAY DIFFRACTION (2 Å)