4PQG

Crystal structure of the pneumococcal O-GlcNAc transferase GtfA in complex with UDP and GlcNAc

Summary for 4PQG

• Entry DOI: 10.2210/pdb4pqg/pdb
• Descriptor: Glycosyltransferase Gtf1, URIDINE-5'-DIPHOSPHATE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: o-glcnac transferase, gt-b fold, rossmann fold, gtfb, transferase
• Biological source: Streptococcus pneumoniae
• Cellular location: Cytoplasm: Q97P84
• Total number of polymer chains: 2
• Total formula weight: 118970.18

Authors

Shi, W.W.,Jiang, Y.L.,Zhu, F.,Yang, Y.H.,Wu, H.,Ren, Y.M.,Chen, Y.,Zhou, C.Z. (deposition date: 2014-03-03, release date: 2014-06-18, Last modification date: 2024-02-28)

Primary citation

Shi, W.W.,Jiang, Y.L.,Zhu, F.,Yang, Y.H.,Shao, Q.Y.,Yang, H.B.,Ren, Y.M.,Wu, H.,Chen, Y.,Zhou, C.Z.
Structure of a Novel O-Linked N-Acetyl-d-glucosamine (O-GlcNAc) Transferase, GtfA, Reveals Insights into the Glycosylation of Pneumococcal Serine-rich Repeat Adhesins.
J.Biol.Chem., 289:20898-20907, 2014

PubMed Abstract: Protein glycosylation catalyzed by the O-GlcNAc transferase (OGT) plays a critical role in various biological processes. In Streptococcus pneumoniae, the core enzyme GtfA and co-activator GtfB form an OGT complex to glycosylate the serine-rich repeat (SRR) of adhesin PsrP (pneumococcal serine-rich repeat protein), which is involved in the infection and pathogenesis. Here we report the 2.0 Å crystal structure of GtfA, revealing a β-meander add-on domain beyond the catalytic domain. It represents a novel add-on domain, which is distinct from the all-α-tetratricopeptide repeats in the only two structure-known OGTs. Structural analyses combined with binding assays indicate that this add-on domain contributes to forming an active GtfA-GtfB complex and recognizing the acceptor protein. In addition, the in vitro glycosylation system enables us to map the O-linkages to the serine residues within the first SRR of PsrP. These findings suggest that fusion with an add-on domain might be a universal mechanism for diverse OGTs that recognize varying acceptor proteins/peptides.

PubMed: 24936067
DOI: 10.1074/jbc.M114.581934

Experimental method

X-RAY DIFFRACTION (2 Å)