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<StructureSection load='6ejk' size='340' side='right' caption='[[6ejk]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='6ejk' size='340' side='right' caption='[[6ejk]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ejk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EJK FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ejk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EJK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=BUE:NerylNeryl+pyrophosphate'>BUE</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=UDN:Uridine-Diphosphate-Methylene-N-acetyl-galactosamine'>UDN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=BUE:NerylNeryl+pyrophosphate'>BUE</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=UDN:Uridine-Diphosphate-Methylene-N-acetyl-galactosamine'>UDN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ejj|6ejj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ejj|6ejj]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wlaC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 "Campylobacter fetus subsp. jejuni" Smibert 1974])</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=6ejk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejk OCA], [http://pdbe.org/6ejk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ejk RCSB], [http://www.ebi.ac.uk/pdbsum/6ejk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejk 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=6ejk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejk OCA], [http://pdbe.org/6ejk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ejk RCSB], [http://www.ebi.ac.uk/pdbsum/6ejk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The membrane-associated, processive and retaining glycosyltransferase PglH from Campylobacter jejuni is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Using an unknown counting mechanism, PglH catalyzes the transfer of exactly three alpha1,4 N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-alpha1,4-GalNAc-alpha1,3-Bac-alpha1-PP-undecaprenyl. Here, we present crystal structures of PglH in three distinct states, including a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated LLO analog and either UDP or synthetic, nonhydrolyzable UDP-CH2-GalNAc. PglH contains an amphipathic helix ("ruler helix") that has a dual role of facilitating membrane attachment and glycan counting. The ruler helix contains three positively charged side chains that can bind the pyrophosphate group of the LLO substrate and thus limit the addition of GalNAc units to three. These results, combined with molecular dynamics simulations, provide the mechanism of glycan counting by PglH. | |||
Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase.,Ramirez AS, Boilevin J, Mehdipour AR, Hummer G, Darbre T, Reymond JL, Locher KP Nat Commun. 2018 Jan 31;9(1):445. doi: 10.1038/s41467-018-02880-2. PMID:29386647<ref>PMID:29386647</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ejk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Campylobacter fetus subsp. jejuni smibert 1974]] | |||
[[Category: Boilevin, J]] | [[Category: Boilevin, J]] | ||
[[Category: Darbre, T]] | [[Category: Darbre, T]] | ||
Latest revision as of 10:08, 15 February 2018
Structure of a glycosyltransferaseStructure of a glycosyltransferase
Structural highlights
Publication Abstract from PubMedThe membrane-associated, processive and retaining glycosyltransferase PglH from Campylobacter jejuni is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Using an unknown counting mechanism, PglH catalyzes the transfer of exactly three alpha1,4 N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-alpha1,4-GalNAc-alpha1,3-Bac-alpha1-PP-undecaprenyl. Here, we present crystal structures of PglH in three distinct states, including a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated LLO analog and either UDP or synthetic, nonhydrolyzable UDP-CH2-GalNAc. PglH contains an amphipathic helix ("ruler helix") that has a dual role of facilitating membrane attachment and glycan counting. The ruler helix contains three positively charged side chains that can bind the pyrophosphate group of the LLO substrate and thus limit the addition of GalNAc units to three. These results, combined with molecular dynamics simulations, provide the mechanism of glycan counting by PglH. Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase.,Ramirez AS, Boilevin J, Mehdipour AR, Hummer G, Darbre T, Reymond JL, Locher KP Nat Commun. 2018 Jan 31;9(1):445. doi: 10.1038/s41467-018-02880-2. PMID:29386647[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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