PDBsum entry 4q3c

Oxidoreductase

PDB id: 4q3c

Contents

Protein chains

259 a.a.

Ligands

NAD ×4

2YG ×4

GOL ×4

EDO ×3

PEG

Metals

_NA ×4

_MG ×4

Waters ×273

PDB id:

4q3c

Name:

Oxidoreductase

Title:

Pyld cocrystallized with l-lysine-ne-l-lysine and NAD+

Structure:

Pyld, pyrrolysine synthase. Chain: a, b, c, d. Engineered: yes

Source:

Methanosarcina barkeri. Organism_taxid: 269797. Strain: fusaro. Gene: mbar_a0835. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.10Å R-factor: 0.170 R-free: 0.198

Authors:

F.Quitterer,P.Beck,A.Bacher,M.Groll

Key ref:

F.Quitterer et al. (2014). The formation of pyrroline and tetrahydropyridine rings in amino acids catalyzed by pyrrolysine synthase (PylD). Angew Chem Int Ed Engl, 53, 8150-8153. PubMed id: 24916332 DOI: 10.1002/anie.201402595

Date:

11-Apr-14 Release date: 23-Apr-14

Protein chains

Q46E80  (PYLD_METBF) -  Pyrrolysine synthase from Methanosarcina barkeri (strain Fusaro / DSM 804)

Seq: 263 a.a.

Struc: 259 a.a.

Enzyme reactions

• Enzyme class: E.C.1.4.1.- - ?????

DOI no: 10.1002/anie.201402595

Angew Chem Int Ed Engl 53:8150-8153 (2014)

PubMed id: 24916332

The formation of pyrroline and tetrahydropyridine rings in amino acids catalyzed by pyrrolysine synthase (PylD).

F.Quitterer, P.Beck, A.Bacher, M.Groll.

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.