3rhz

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Current revision (09:42, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3rhz' size='340' side='right'caption='[[3rhz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3rhz' size='340' side='right'caption='[[3rhz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rhz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_15912 Atcc 15912]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RHZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rhz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_parasanguinis Streptococcus parasanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RHZ 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=CL:CHLORIDE+ION'>CL</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]] 1.898&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nss ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1318 ATCC 15912])</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=CL:CHLORIDE+ION'>CL</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=3rhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rhz OCA], [https://pdbe.org/3rhz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rhz RCSB], [https://www.ebi.ac.uk/pdbsum/3rhz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rhz 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=3rhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rhz OCA], [https://pdbe.org/3rhz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rhz RCSB], [https://www.ebi.ac.uk/pdbsum/3rhz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rhz ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/GTF3_STRPA GTF3_STRPA] Required for polymorphic O-glycosylation of the serine-rich repeat protein Fap1. Catalyzes the second step in glycosylation of the serine-rich repeat protein in this bacteria. Transfers glucose from UDP-glucose to the terminal GlcNAc moiety of 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl-[protein] which results from the first glycosylation step of Fap1; does not use other sugar nucleotides as substrates.<ref>PMID:20164186</ref> <ref>PMID:21653318</ref> <ref>PMID:25404702</ref>
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Serine-rich repeat glycoproteins (SRRPs) are a growing family of bacterial adhesins found in many streptococci and staphylococci; they play important roles in bacterial biofilm formation and pathogenesis. Glycosylation of this family of adhesins is essential for their biogenesis. A glucosyltransferase (Gtf3) catalyzes the second step of glycosylation of a SRRP (Fap1) from an oral streptococcus, Streptococcus parasanguinis. Although Gtf3 homologs are highly conserved in SRRP-containing streptococci, they share minimal homology with functionally known glycosyltransferases. We report here the 2.3 A crystal structure of Gtf3. The structural analysis indicates that Gtf3 forms a tetramer and shares significant structural homology with glycosyltransferases from GT4, GT5, and GT20 subfamilies. Combining crystal structural analysis with site-directed mutagenesis and in vitro glycosyltransferase assays, we identified residues that are required for UDP or UDP-Glucose binding and for oligomerization of Gtf3, and determined their contribution to the enzymatic activity of Gtf3. Further in vivo studies revealed that the critical amino acid residues identified by the structural analysis are crucial for Fap1 glycosylation in S. parasanguinis in vivo. Moreover, Gtf3 homologs from other streptococci were able to rescue the gtf3 knockout mutant of S. parasanguinis in vivo and catalyze the sugar transfer to the modified SRRP substrate in vitro, demonstrating the importance and conservation of the Gtf3 homologs in glycosylation of SRRPs. As the Gtf3 homologs only exist in SRRP-containing streptococci, we conclude that the Gtf3 homologs represent a unique subfamily of glycosyltransferases.
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Structural and functional analysis of a new subfamily of glycosyltransferases required for glycosylation of serine-rich streptococcal adhesins.,Zhu F, Erlandsen H, Ding L, Li J, Huang Y, Zhou M, Liang X, Ma J, Wu H J Biol Chem. 2011 Jun 7. PMID:21653318<ref>PMID:21653318</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 3rhz" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 15912]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, J]]
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[[Category: Streptococcus parasanguinis]]
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[[Category: Wu, H]]
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[[Category: Li J]]
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[[Category: Zhu, F]]
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[[Category: Wu H]]
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[[Category: Glycosyltransferase]]
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[[Category: Zhu F]]
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[[Category: Transferase]]
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Current revision

Structure and functional analysis of a new subfamily of glycosyltransferases required for glycosylation of serine-rich streptococcal adhesions

PDB ID 3rhz

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