5VVU

Structural Investigations of the Substrate Specificity of Human O-GlcNAcase

Summary for 5VVU

• Entry DOI: 10.2210/pdb5vvu/pdb
• Related: 5VVO 5VVT 5VVV 5VVX
• Descriptor: Protein O-GlcNAcase, TAB1 peptide, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: oga, human o-glcnacase, hydrolase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 117589.17

Authors

Li, B.,Jiang, J.,Li, H.,Hu, C.-W. (deposition date: 2017-05-20, release date: 2017-09-27, Last modification date: 2024-10-23)

Primary citation

Li, B.,Li, H.,Hu, C.W.,Jiang, J.
Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.
Nat Commun, 8:666-666, 2017

PubMed Abstract: The O-linked β-N-acetyl glucosamine (O-GlcNAc) modification dynamically regulates the functions of numerous proteins. A single human enzyme O-linked β-N-acetyl glucosaminase (O-GlcNAcase or OGA) hydrolyzes this modification. To date, it remains largely unknown how OGA recognizes various substrates. Here we report the structures of OGA in complex with each of four distinct glycopeptide substrates that contain a single O-GlcNAc modification on a serine or threonine residue. Intriguingly, these glycopeptides bind in a bidirectional yet conserved conformation within the substrate-binding cleft of OGA. This study provides fundamental insights into a general principle that confers the substrate binding adaptability and specificity to OGA in O-GlcNAc regulation.O-linked β-N-acetyl glucosamine (O-GlcNAc) is an important protein modification that is hydrolyzed by O-GlcNAcase (OGA). Here the authors give insights into OGA substrate recognition by presenting four human OGA structures complexed with glycopeptide substrates containing a single O-GlcNAc modification on either a serine or threonine.

PubMed: 28939839
DOI: 10.1038/s41467-017-00865-1

Experimental method

X-RAY DIFFRACTION (2.7 Å)