6P78
queuine lyase from Clostridium spiroforme bound to SAM and queuine
Summary for 6P78
| Entry DOI | 10.2210/pdb6p78/pdb |
| Descriptor | 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) |
| Functional Keywords | metal ion binding, 4 iron 4 sulfur cluster binding, radical sam enzyme, c-n lyase activity, lyase |
| Biological source | [Clostridium] spiroforme DSM 1552 |
| Total number of polymer chains | 1 |
| Total formula weight | 30961.44 |
| Authors | Almo, S.C.,Grove, T.L. (deposition date: 2019-06-05, release date: 2019-09-18, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 31481610DOI: 10.1073/pnas.1909604116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.726 Å) |
Structure validation
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