<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Griffiths R</submitter><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>708-717</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12809243</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>81(Pt 12)</volume><pubmed_abstract>The accessory secretion (aSec) system is a protein export pathway that is uniquely present in Gram-positive bacteria and is dedicated to the secretion of large, glycosylated cell wall-anchored adhesins called serine-rich repeat proteins (SRRPs). Strain-specific glycosylation of SRRPs has previously been reported in Limosilactobacillus reuteri and attributed to GtfC, a glycosyltransferase belonging to family 113, with LrGtfC&lt;sub>100-23&lt;/sub> from L. reuteri rat strain 100-23C showing specificity for UDP-Glc, while LrGtfC&lt;sub>53608&lt;/sub> from L. reuteri pig strain ATCC 53608, which differs at only ten amino-acid positions, shows a preference for UDP-GlcNAc. However, the structural basis underpinning GtfC sugar-donor specificity remains unclear. Here, we report X-ray crystal structures of the</pubmed_abstract><journal>Acta crystallographica. Section D, Structural biology</journal><pubmed_title>A structural basis for the strain-dependent UDP-sugar specificity of glycosyltransferase C from the Limosilactobacillus reuteri accessory secretion system.</pubmed_title><pmcid>PMC12809243</pmcid><funding_grant_id>BB/R012490/1</funding_grant_id><funding_grant_id>BB/X011054/1</funding_grant_id><funding_grant_id>BB/M011216/1</funding_grant_id><pubmed_authors>Juge N</pubmed_authors><pubmed_authors>Griffiths R</pubmed_authors><pubmed_authors>Ashworth G</pubmed_authors><pubmed_authors>Hemmings A</pubmed_authors><pubmed_authors>Pfalzgraf H</pubmed_authors><pubmed_authors>Dong C</pubmed_authors><pubmed_authors>Latousakis D</pubmed_authors></additional><is_claimable>false</is_claimable><name>A structural basis for the strain-dependent UDP-sugar specificity of glycosyltransferase C from the Limosilactobacillus reuteri accessory secretion system.</name><description>The accessory secretion (aSec) system is a protein export pathway that is uniquely present in Gram-positive bacteria and is dedicated to the secretion of large, glycosylated cell wall-anchored adhesins called serine-rich repeat proteins (SRRPs). Strain-specific glycosylation of SRRPs has previously been reported in Limosilactobacillus reuteri and attributed to GtfC, a glycosyltransferase belonging to family 113, with LrGtfC&lt;sub>100-23&lt;/sub> from L. reuteri rat strain 100-23C showing specificity for UDP-Glc, while LrGtfC&lt;sub>53608&lt;/sub> from L. reuteri pig strain ATCC 53608, which differs at only ten amino-acid positions, shows a preference for UDP-GlcNAc. However, the structural basis underpinning GtfC sugar-donor specificity remains unclear. Here, we report X-ray crystal structures of the</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Dec</publication><modification>2026-06-06T16:02:40.725Z</modification><creation>2026-06-02T03:09:49.864Z</creation></dates><accession>S-EPMC12809243</accession><cross_references><pubmed>41190658</pubmed><doi>10.1107/S2059798325008782</doi></cross_references></HashMap>