PDBsum entry 4zfl

Hydrolase

PDB id: 4zfl

Contents

Protein chains

(+ 6 more) 229 a.a.

Ligands

4NK ×12

GOL ×4

Waters ×3083

PDB id:

4zfl

Name:

Hydrolase

Title:

Ergothioneine-biosynthetic ntn hydrolase variant egtc_c2a with natural substrate

Structure:

Amidohydrolase egtc. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Engineered: yes. Mutation: yes

Source:

Mycobacterium smegmatis (strain atcc 700084 / mc(2)155). Organism_taxid: 246196. Gene: egtc, msmeg_6248, msmei_6087. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.70Å R-factor: 0.145 R-free: 0.171

Authors:

A.Vit,F.P.Seebeck,W.Blankenfeldt

Key ref:

A.Vit et al. (2015). Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC. Chembiochem, 16, 1490-1496. PubMed id: 26079795 DOI: 10.1002/cbic.201500168

Date:

21-Apr-15 Release date: 01-Jul-15

Protein chains

A0R5M9  (EGTC_MYCS2) -  Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

Seq: 227 a.a.

Struc: 229 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.5.1.118 - gamma-glutamyl hercynylcysteine S-oxide hydrolase.
• Reaction: gamma-L-glutamyl-hercynylcysteine S-oxide + H2O = S-(hercyn-2-yl)-L- cysteine S-oxide + L-glutamate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

DOI no: 10.1002/cbic.201500168

Chembiochem 16:1490-1496 (2015)

PubMed id: 26079795

Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC.

A.Vit, G.T.Mashabela, W.Blankenfeldt, F.P.Seebeck.

ABSTRACT

The ubiquitous sulfur metabolite ergothioneine is biosynthesized by oxidative attachment of a sulfur atom to the imidazole ring of Nα-trimethylhistidine. Most actinobacteria, including Mycobacterium tuberculosis, use γ-glutamyl cysteine as a sulfur donor. In subsequent steps the carbon scaffold of γ-glutamyl cysteine is removed by the glutamine amidohydrolase EgtC and the β-lyase EgtE. We determined the crystal structure of EgtC from Mycobacterium smegmatis in complex with its physiological substrate. The set of active site residues that define substrate specificity in EgtC are highly conserved, even in homologues that are not involved in ergothioneine production. This conservation is compounded by the phylogenetic distribution of EgtC-like enzymes indicates that their last common ancestor might have emerged for a purpose other than ergothioneine production.