PDBsum entry 6b1v

Hydrolase

PDB id: 6b1v

Contents

Protein chains

452 a.a.

Ligands

G4S-DGS-G4S-DGS ×5

EDO

Metals

_CA ×3

Waters ×64

PDB id:

6b1v

Name:

Hydrolase

Title:

Crystal structure of ps i-cgsb c78s in complex with i-neocarratetraose

Structure:

Iota-carrageenan sulfatase. Chain: a, b, c. Engineered: yes

Source:

Pseudoalteromonas. Organism_taxid: 53246. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.84Å R-factor: 0.235 R-free: 0.264

Authors:

A.G.Hettle,A.B.Boraston

Key ref:

A.G.Hettle et al. (2018). The Molecular Basis of Polysaccharide Sulfatase Activity and a Nomenclature for Catalytic Subsites in this Class of Enzyme. Structure, 26, 747. PubMed id: 29681469 DOI: 10.1016/j.str.2018.03.012

Date:

19-Sep-17 Release date: 14-Mar-18

Protein chains

No UniProt id for this chain

Struc: 452 a.a.

DOI no: 10.1016/j.str.2018.03.012

Structure 26:747 (2018)

PubMed id: 29681469

The Molecular Basis of Polysaccharide Sulfatase Activity and a Nomenclature for Catalytic Subsites in this Class of Enzyme.

A.G.Hettle, C.Vickers, C.S.Robb, F.Liu, S.G.Withers, J.H.Hehemann, A.B.Boraston.

ABSTRACT

Sulfatases play a biologically important role by cleaving sulfate groups from molecules. They can be identified on the basis of signature sequences within their primary structures, and the largest family, S1, has predictable features that contribute specifically to the recognition and catalytic removal of sulfate groups. However, despite advances in the prediction and understanding of S1 sulfatases, a major question regards the molecular determinants that drive substrate recognition beyond the targeted sulfate group. Here, through analysis of an endo-4S-ι-carrageenan sulfatase (PsS1_19A) from Pseudoalteromonas sp. PS47, particularly X-ray crystal structures in complex with intact substrates, we show that specific recognition of the substrate leaving group components, in this case carbohydrate, provides the enzyme with specificity for its substrate. On the basis of these results we propose a catalytic subsite nomenclature that we anticipate will form a general foundation for understanding and describing the molecular basis of substrate recognition by sulfatases.