4EVZ

Structure of HisF-LUCA

4EVZ の概要

• エントリーDOI: 10.2210/pdb4evz/pdb
• 分子名称: HisF-LUCA, HYDROGENPHOSPHATE ION (3 entities in total)
• 機能のキーワード: imidazole glycerol phosphate synthase-luca, lyase
• 由来する生物種: artificial gene
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56222.80

構造登録者

Reisinger, B.,Sperl, J.,Rajendran, C.,Merkl, R.,Sterner, R. (登録日: 2012-04-26, 公開日: 2013-11-06, 最終更新日: 2023-09-13)

主引用文献

Reisinger, B.,Sperl, J.,Holinski, A.,Schmid, V.,Rajendran, C.,Carstensen, L.,Schlee, S.,Blanquart, S.,Merkl, R.,Sterner, R.
Evidence for the existence of elaborate enzyme complexes in the Paleoarchean era.
J.Am.Chem.Soc., 136:122-129, 2014

PubMed Abstract: Due to the lack of macromolecular fossils, the enzymatic repertoire of extinct species has remained largely unknown to date. In an attempt to solve this problem, we have characterized a cyclase subunit (HisF) of the imidazole glycerol phosphate synthase (ImGP-S), which was reconstructed from the era of the last universal common ancestor of cellular organisms (LUCA). As observed for contemporary HisF proteins, the crystal structure of LUCA-HisF adopts the (βα)8-barrel architecture, one of the most ancient folds. Moreover, LUCA-HisF (i) resembles extant HisF proteins with regard to internal 2-fold symmetry, active site residues, and a stabilizing salt bridge cluster, (ii) is thermostable and shows a folding mechanism similar to that of contemporary (βα)8-barrel enzymes, (iii) displays high catalytic activity, and (iv) forms a stable and functional complex with the glutaminase subunit (HisH) of an extant ImGP-S. Furthermore, we show that LUCA-HisF binds to a reconstructed LUCA-HisH protein with high affinity. Our findings suggest that the evolution of highly efficient enzymes and enzyme complexes has already been completed in the LUCA era, which means that sophisticated catalytic concepts such as substrate channeling and allosteric communication existed already 3.5 billion years ago.

PubMed: 24364418
DOI: 10.1021/ja4115677

実験手法

X-RAY DIFFRACTION (1.462 Å)