6B1V

Crystal structure of Ps i-CgsB C78S in complex with i-neocarratetraose

Summary for 6B1V

• Entry DOI: 10.2210/pdb6b1v/pdb
• Related: 6B0J 6B0K
• Descriptor: Iota-carrageenan sulfatase, 3,6-anhydro-2-O-sulfo-alpha-D-galactopyranose-(1-3)-4-O-sulfo-beta-D-galactopyranose-(1-4)-3,6-anhydro-2-O-sulfo-alpha-D-galactopyranose-(1-3)-4-O-sulfo-beta-D-galactopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: s1 sulfatase, hydrolase
• Biological source: Pseudoalteromonas
• Total number of polymer chains: 3
• Total formula weight: 158952.70

Authors

Hettle, A.G.,Boraston, A.B. (deposition date: 2017-09-19, release date: 2018-03-14, Last modification date: 2023-10-04)

Primary citation

Hettle, A.G.,Vickers, C.,Robb, C.S.,Liu, F.,Withers, S.G.,Hehemann, J.H.,Boraston, A.B.
The Molecular Basis of Polysaccharide Sulfatase Activity and a Nomenclature for Catalytic Subsites in this Class of Enzyme.
Structure, 26:747-, 2018

PubMed 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.

PubMed: 29681469
DOI: 10.1016/j.str.2018.03.012

Experimental method

X-RAY DIFFRACTION (2.84 Å)