1IGW

Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli

1IGW の概要

• エントリーDOI: 10.2210/pdb1igw/pdb
• 分子名称: Isocitrate lyase, MERCURY (II) ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: beta barrel, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 195055.44

構造登録者

Britton, K.L.,Abeysinghe, I.S.B.,Baker, P.J.,Barynin, V.,Diehl, P.,Langridge, S.J.,McFadden, B.A.,Sedelnikova, S.E.,Stillman, T.J.,Weeradechapon, K.,Rice, D.W. (登録日: 2001-04-18, 公開日: 2001-09-05, 最終更新日: 2023-11-15)

主引用文献

Britton, K.L.,Abeysinghe, I.S.,Baker, P.J.,Barynin, V.,Diehl, P.,Langridge, S.J.,McFadden, B.A.,Sedelnikova, S.E.,Stillman, T.J.,Weeradechapon, K.,Rice, D.W.
The structure and domain organization of Escherichia coli isocitrate lyase.
Acta Crystallogr.,Sect.D, 57:1209-1218, 2001

PubMed Abstract: Enzymes of the glyoxylate-bypass pathway are potential targets for the control of many human diseases caused by such pathogens as Mycobacteria and Leishmania. Isocitrate lyase catalyses the first committed step in this pathway and the structure of this tetrameric enzyme from Escherichia coli has been determined at 2.1 A resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found localized in glyoxysomes. Comparison of the structure of the prokaryotic isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals a different domain structure following the deletion of approximately 100 residues from the larger eukaryotic enzyme. Despite this, the active sites of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein that are known to be involved in a conformational change as part of the enzyme's catalytic cycle.

PubMed: 11526312
DOI: 10.1107/S0907444901008642

実験手法

X-RAY DIFFRACTION (2.1 Å)