4pqg

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4pqg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PQG FirstGlance]. <br>
<table><tr><td colspan='2'>[[4pqg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PQG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqg OCA], [https://pdbe.org/4pqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pqg RCSB], [https://www.ebi.ac.uk/pdbsum/4pqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pqg ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqg OCA], [https://pdbe.org/4pqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pqg RCSB], [https://www.ebi.ac.uk/pdbsum/4pqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pqg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/GTFA_STRPN GTFA_STRPN] Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP (PubMed:24936067, PubMed:28246170). Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues (PubMed:24936067). The alpha linkage was shown in L.reuteri.[UniProtKB:A0A0S4NM89]<ref>PMID:24936067</ref> <ref>PMID:28246170</ref> <ref>PMID:16861665</ref>
[https://www.uniprot.org/uniprot/GTFA_STRPN GTFA_STRPN] Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP (PubMed:24936067, PubMed:28246170). Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues (PubMed:24936067). The alpha linkage was shown in L.reuteri.[UniProtKB:A0A0S4NM89]<ref>PMID:24936067</ref> <ref>PMID:28246170</ref> <ref>PMID:16861665</ref>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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 A crystal structure of GtfA, revealing a beta-meander add-on domain beyond the catalytic domain. It represents a novel add-on domain, which is distinct from the all-alpha-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.
 
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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.,Shi WW, Jiang YL, Zhu F, Yang YH, Shao QY, Yang HB, Ren YM, Wu H, Chen Y, Zhou CZ J Biol Chem. 2014 Jul 25;289(30):20898-20907. Epub 2014 Jun 16. PMID:24936067<ref>PMID:24936067</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 4pqg" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==

Current revision

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

PDB ID 4pqg

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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