4ZXL

CpOGA D298N in complex with Drosophila HCF -derived Thr-O-GlcNAc peptide

Summary for 4ZXL

• Entry DOI: 10.2210/pdb4zxl/pdb
• Related: 2VUR 2YDQ 2YDR 2YDS
• Descriptor: NAG-PRO-SER-THR-ALA-Thr-O-GlcNAc containing peptide from drosophila HCF, O-GlcNAcase NagJ, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: hydrolase-o-glcnacylated peptide complex tim barrel thr-o-glcnac, hydrolase-peptide complex, hydrolase/peptide
• Biological source: Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A); More
• Total number of polymer chains: 2
• Total formula weight: 67381.70

Authors

Selvan, N.,van Aalten, D.M.F. (deposition date: 2015-05-20, release date: 2015-09-23, Last modification date: 2024-11-06)

Primary citation

Mariappa, D.,Selvan, N.,Borodkin, V.S.,Alonso, J.,Ferenbach, A.T.,Shepherd, C.,Navratilova, I.H.,van Aalten, D.M.
A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development.
Biochem.J., 470:255-262, 2015

PubMed Abstract: O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-N-acetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.

PubMed: 26348912
DOI: 10.1042/BJ20150610

Experimental method

X-RAY DIFFRACTION (2.6 Å)