4pqg

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(Difference between revisions)

Revision as of 07:24, 8 February 2023

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

Structural highlights

4pqg is a 2 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]^[1] ^[2] ^[3]

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shi WW, Jiang YL, Zhu F, Yang YH, Shao QY, Yang HB, Ren YM, Wu H, Chen Y, Zhou CZ. 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. 2014 Jul 25;289(30):20898-20907. Epub 2014 Jun 16. PMID:24936067 doi:http://dx.doi.org/10.1074/jbc.M114.581934
↑ Jiang YL, Jin H, Yang HB, Zhao RL, Wang S, Chen Y, Zhou CZ. Defining the enzymatic pathway for polymorphic O-glycosylation of the pneumococcal serine-rich repeat protein PsrP. J Biol Chem. 2017 Apr 14;292(15):6213-6224. doi: 10.1074/jbc.M116.770446. Epub, 2017 Feb 28. PMID:28246170 doi:http://dx.doi.org/10.1074/jbc.M116.770446
↑ Obert C, Sublett J, Kaushal D, Hinojosa E, Barton T, Tuomanen EI, Orihuela CJ. Identification of a Candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease. Infect Immun. 2006 Aug;74(8):4766-77. PMID:16861665 doi:10.1128/IAI.00316-06
↑ Shi WW, Jiang YL, Zhu F, Yang YH, Shao QY, Yang HB, Ren YM, Wu H, Chen Y, Zhou CZ. 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. 2014 Jul 25;289(30):20898-20907. Epub 2014 Jun 16. PMID:24936067 doi:http://dx.doi.org/10.1074/jbc.M114.581934

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4pqg"

@@ Line 3: / Line 3: @@
 <StructureSection load='4pqg' size='340' side='right'caption='[[4pqg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4pqg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. 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 [http://oca.weizmann.ac.il/oca-docs/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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
+</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>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gtf1, SP_1758 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqg OCA], [http://pdbe.org/4pqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pqg RCSB], [http://www.ebi.ac.uk/pdbsum/4pqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pqg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q97P84_STRPN Q97P84_STRPN]] An N-acetylglucosaminyl transferase that is part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins usually encoded upstream in the same operon (By similarity).[HAMAP-Rule:MF_01472]
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 20: @@
 ==See Also==
-*[[Glycosyltransferase|Glycosyltransferase]]
+*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
-*[[O-GlcNAc transferase|O-GlcNAc transferase]]
+*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]]
 == References ==
 <references/>
@@ Line 28: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Strpn]]
+[[Category: Streptococcus pneumoniae TIGR4]]
-[[Category: Chen, Y]]
+[[Category: Chen Y]]
-[[Category: Jiang, Y L]]
+[[Category: Jiang YL]]
-[[Category: Ren, Y M]]
+[[Category: Ren YM]]
-[[Category: Shi, W W]]
+[[Category: Shi WW]]
-[[Category: Wu, H]]
+[[Category: Wu H]]
-[[Category: Yang, Y H]]
+[[Category: Yang YH]]
-[[Category: Zhou, C Z]]
+[[Category: Zhou CZ]]
-[[Category: Zhu, F]]
+[[Category: Zhu F]]
-[[Category: Gt-b fold]]
-[[Category: Gtfb]]
-[[Category: O-glcnac transferase]]
-[[Category: Rossmann fold]]
-[[Category: Transferase]]

4pqg

From Proteopedia

Revision as of 07:24, 8 February 2023

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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