ISDA: 5NYY

Deposition Date 2017-05-12

Release Date 2017-06-07

Last Version Date 2024-01-17

Entry Detail

PDB ID:

5NYY

Keywords:

TRANSFERASE

Title:

Formylglycine generating enzyme from T. curvata in complex with Cd(II)

Biological Source:

Source Organism(s):

Thermomonospora curvata DSM 43183 (Taxon ID: 471852)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.28 Å

R-Value Free:

0.16

R-Value Work:

0.15

R-Value Observed:

0.15

Space Group:

P 21 21 21

Download Validation Report

Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Non-specific serine/threonine
Gene (Uniprot):Tcur_4811
Chain IDs:A
Chain Length:300
Number of Molecules:1
Biological Source:Thermomonospora curvata DSM 43183

UniProt ID:D1A7C3 Pfam ID:PF03781 EC:2.7.11.1

Ligand Molecules

ACT

MPD

MRD

Primary Citation

Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme.

Meury, M, Knop, M, Seebeck, F.P.Show

Angew. Chem. Int. Ed. Engl. 56 8115 8119 (2017)

PMID: 28544744 DOI: 10.1002/anie.201702901

Abstact

The formylglycine-generating enzyme (FGE) is a unique copper protein that catalyzes oxygen-dependent C-H activation. We describe 1.66 Å- and 1.28 Å-resolution crystal structures of FGE from Thermomonospora curvata in complex with either AgI or CdII providing definitive evidence for a high-affinity metal-binding site in this enzyme. The structures reveal a bis-cysteine linear coordination of the monovalent metal, and tetrahedral coordination of the bivalent metal. Similar coordination changes may occur in the active enzyme as a result of CuI/II redox cycling. Complexation of copper atoms by two cysteine residues is common among copper-trafficking proteins, but is unprecedented for redox-active copper enzymes or synthetic copper catalysts.

Legend

Protein

Chemical

Disease

Primary Citation of related structures

Abstact

Feedback Form