6P78

queuine lyase from Clostridium spiroforme bound to SAM and queuine

6P78 の概要

• エントリーDOI: 10.2210/pdb6p78/pdb
• 分子名称: Queuine lyase, IRON/SULFUR CLUSTER, 2-amino-5-({[(1S,4S,5S)-4,5-dihydroxycyclopent-2-en-1-yl]amino}methyl)-1,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one, ... (5 entities in total)
• 機能のキーワード: metal ion binding, 4 iron 4 sulfur cluster binding, radical sam enzyme, c-n lyase activity, lyase
• 由来する生物種: [Clostridium] spiroforme DSM 1552
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30961.44

構造登録者

Almo, S.C.,Grove, T.L. (登録日: 2019-06-05, 公開日: 2019-09-18, 最終更新日: 2024-10-30)

主引用文献

Yuan, Y.,Zallot, R.,Grove, T.L.,Payan, D.J.,Martin-Verstraete, I.,Sepic, S.,Balamkundu, S.,Neelakandan, R.,Gadi, V.K.,Liu, C.F.,Swairjo, M.A.,Dedon, P.C.,Almo, S.C.,Gerlt, J.A.,de Crecy-Lagard, V.
Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens.
Proc.Natl.Acad.Sci.USA, 116:19126-19135, 2019

PubMed Abstract: Queuosine (Q) is a complex tRNA modification widespread in eukaryotes and bacteria that contributes to the efficiency and accuracy of protein synthesis. Eukaryotes are not capable of Q synthesis and rely on salvage of the queuine base (q) as a Q precursor. While many bacteria are capable of Q de novo synthesis, salvage of the prokaryotic Q precursors preQ and preQ also occurs. With the exception of YhhQ, shown to transport preQ and preQ, the enzymes and transporters involved in Q salvage and recycling have not been well described. We discovered and characterized 2 Q salvage pathways present in many pathogenic and commensal bacteria. The first, found in the intracellular pathogen , uses YhhQ and tRNA guanine transglycosylase (TGT) homologs that have changed substrate specificities to directly salvage q, mimicking the eukaryotic pathway. The second, found in bacteria from the gut flora such as , salvages preQ from q through an unprecedented reaction catalyzed by a newly defined subgroup of the radical-SAM enzyme family. The source of q can be external through transport by members of the energy-coupling factor (ECF) family or internal through hydrolysis of Q by a dedicated nucleosidase. This work reinforces the concept that hosts and members of their associated microbiota compete for the salvage of Q precursors micronutrients.

PubMed: 31481610
DOI: 10.1073/pnas.1909604116

実験手法

X-RAY DIFFRACTION (1.726 Å)