8GR2

Crystal structure of the GDSL-family esterase CJ0610C from Campylobacter jejuni

Summary for 8GR2

• Entry DOI: 10.2210/pdb8gr2/pdb
• Descriptor: DUF459 domain-containing protein, SULFATE ION (3 entities in total)
• Functional Keywords: gdsl-family esterase, hydrolase
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 1
• Total formula weight: 26401.06

Authors

Ki, D.U.,Song, W.S.,Yoon, S.I. (deposition date: 2022-08-31, release date: 2022-11-16, Last modification date: 2024-04-03)

Primary citation

Ki, D.U.,Song, W.S.,Yoon, S.I.
Structural and biochemical analysis of the GDSL-family esterase CJ0610C from Campylobacter jejuni.
Biochem.Biophys.Res.Commun., 631:124-129, 2022

PubMed Abstract: GDSL domain-containing proteins generally hydrolyze esters or lipids and play critical roles in diverse biological and industrial processes. GDSL hydrolases use catalytic triad and oxyanion hole residues from conserved blocks I, II, III, and V to drive the esterase reaction. However, GDSL hydrolases exhibit large deviations in sequence, structure, and substrate specificity, requiring the characterization of each GDSL hydrolase to reveal its catalytic mechanism. We identified a GDSL protein (CJ0610C) from pathogenic Campylobacter jejuni and assessed its biochemical and structural features. CJ0610C displayed esterase activity for p-nitrophenyl acetate and preferred short chain esters and alkaline pH. The C-terminal two-thirds of CJ0610C corresponding to the GDSL domain forms a three-layered α/β/α fold as a core structure in which a five-stranded β-sheet is sandwiched by α-helices. In the CJ0610C structure, conserved catalytic triad and oxyanion hole residues that are indispensable for esterase activity are found in blocks I, III, and V. However, CJ0610C lacks the conserved block-II glycine residue and instead employs a unique asparagine residue as another oxyanion hole residue. Moreover, our structural analysis suggests that substrate binding is mediated by a CJ0610C-specific pocket, which is surrounded by hydrophobic residues and occluded at one end by a positively charged arginine residue.

PubMed: 36183553
DOI: 10.1016/j.bbrc.2022.09.071

Experimental method

X-RAY DIFFRACTION (1.65 Å)