4Q3A

PylD cocrystallized with L-Lysine-Ne-3S-methyl-L-ornithine and NAD+

Summary for 4Q3A

Entry DOI	10.2210/pdb4q3a/pdb
Related	3T7V 4FFP 4Q39 4Q3B 4Q3C 4Q3D 4Q3E
Descriptor	PYLD, pyrrolysine synthase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, SODIUM ION, ... (10 entities in total)
Functional Keywords	rossmann fold, dehydrogenase, pyrrolysine, oxidoreductase
Biological source	Methanosarcina barkeri
Total number of polymer chains	4
Total formula weight	118334.17
Authors	Quitterer, F.,Beck, P.,Bacher, A.,Groll, M. (deposition date: 2014-04-11, release date: 2014-04-23, Last modification date: 2024-10-16)
Primary citation	Quitterer, F.,Beck, P.,Bacher, A.,Groll, M. The Formation of Pyrroline and Tetrahydropyridine Rings in Amino Acids Catalyzed by Pyrrolysine Synthase (PylD). Angew.Chem.Int.Ed.Engl., 53:8150-8153, 2014 Cited by PubMed Abstract: The dehydrogenase PylD catalyzes the ultimate step of the pyrrolysine pathway by converting the isopeptide L-lysine-Nε-3R-methyl-D-ornithine to the 22nd proteinogenic amino acid. In this study, we demonstrate how PylD can be harnessed to oxidize various isopeptides to novel amino acids by combining chemical synthesis with enzyme kinetics and X-ray crystallography. The data enable a detailed description of the PylD reaction trajectory for the biosynthesis of pyrroline and tetrahydropyridine rings as constituents of pyrrolysine analogues. PubMed: 24916332 DOI: 10.1002/anie.201402595 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation