8e37: Difference between revisions
New page: '''Unreleased structure''' The entry 8e37 is ON HOLD Authors: Vuksanovic, N., Ray, L.C., Imperiali, B., Allen, K.N. Description: Structure of Campylobacter concisus wild-type PglC [[Ca... |
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The | ==Structure of Campylobacter concisus wild-type SeMet PglC== | ||
<StructureSection load='8e37' size='340' side='right'caption='[[8e37]], [[Resolution|resolution]] 3.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8e37]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_concisus_13826 Campylobacter concisus 13826]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E37 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=8e37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e37 OCA], [https://pdbe.org/8e37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e37 RCSB], [https://www.ebi.ac.uk/pdbsum/8e37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e37 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A7ZET4_CAMC1 A7ZET4_CAMC1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Complex glycans serve essential functions in all living systems. Many of these intricate and byzantine biomolecules are assembled employing biosynthetic pathways wherein the constituent enzymes are membrane-associated. A signature feature of the stepwise assembly processes is the essentiality of unusual linear long-chain polyprenol phosphate-linked substrates of specific isoprene unit geometry, such as undecaprenol phosphate (UndP) in bacteria. How these enzymes and substrates interact within a lipid bilayer needs further investigation. Here, we focus on a small enzyme, PglC from Campylobacter, structurally characterized for the first time in 2018 as a detergent-solubilized construct. PglC is a monotopic phosphoglycosyl transferase that embodies the functional core structure of the entire enzyme superfamily and catalyzes the first membrane-committed step in a glycoprotein assembly pathway. The size of the enzyme is significant as it enables high-level computation and relatively facile, for a membrane protein, experimental analysis. Our ensemble computational and experimental results provided a high-level view of the membrane-embedded PglC/UndP complex. The findings suggested that it is advantageous for the polyprenol phosphate to adopt a conformation in the same leaflet where the monotopic membrane protein resides as opposed to additionally disrupting the opposing leaflet of the bilayer. Further, the analysis showed that electrostatic steering acts as a major driving force contributing to the recognition and binding of both UndP and the soluble nucleotide sugar substrate. Iterative computational and experimental mutagenesis support a specific interaction of UndP with phosphoglycosyl transferase cationic residues and suggest a role for critical conformational transitions in substrate binding and specificity. | |||
Synergistic computational and experimental studies of a phosphoglycosyl transferase membrane/ligand ensemble.,Majumder A, Vuksanovic N, Ray LC, Bernstein HM, Allen KN, Imperiali B, Straub JE J Biol Chem. 2023 Oct;299(10):105194. doi: 10.1016/j.jbc.2023.105194. Epub 2023 , Aug 25. PMID:37633332<ref>PMID:37633332</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8e37" style="background-color:#fffaf0;"></div> | ||
[[Category: Imperiali | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Campylobacter concisus 13826]] | |||
[[Category: Large Structures]] | |||
[[Category: Allen KN]] | |||
[[Category: Imperiali B]] | |||
[[Category: Ray LC]] | |||
[[Category: Vuksanovic N]] | |||
Latest revision as of 12:49, 9 October 2024
Structure of Campylobacter concisus wild-type SeMet PglCStructure of Campylobacter concisus wild-type SeMet PglC
Structural highlights
FunctionPublication Abstract from PubMedComplex glycans serve essential functions in all living systems. Many of these intricate and byzantine biomolecules are assembled employing biosynthetic pathways wherein the constituent enzymes are membrane-associated. A signature feature of the stepwise assembly processes is the essentiality of unusual linear long-chain polyprenol phosphate-linked substrates of specific isoprene unit geometry, such as undecaprenol phosphate (UndP) in bacteria. How these enzymes and substrates interact within a lipid bilayer needs further investigation. Here, we focus on a small enzyme, PglC from Campylobacter, structurally characterized for the first time in 2018 as a detergent-solubilized construct. PglC is a monotopic phosphoglycosyl transferase that embodies the functional core structure of the entire enzyme superfamily and catalyzes the first membrane-committed step in a glycoprotein assembly pathway. The size of the enzyme is significant as it enables high-level computation and relatively facile, for a membrane protein, experimental analysis. Our ensemble computational and experimental results provided a high-level view of the membrane-embedded PglC/UndP complex. The findings suggested that it is advantageous for the polyprenol phosphate to adopt a conformation in the same leaflet where the monotopic membrane protein resides as opposed to additionally disrupting the opposing leaflet of the bilayer. Further, the analysis showed that electrostatic steering acts as a major driving force contributing to the recognition and binding of both UndP and the soluble nucleotide sugar substrate. Iterative computational and experimental mutagenesis support a specific interaction of UndP with phosphoglycosyl transferase cationic residues and suggest a role for critical conformational transitions in substrate binding and specificity. Synergistic computational and experimental studies of a phosphoglycosyl transferase membrane/ligand ensemble.,Majumder A, Vuksanovic N, Ray LC, Bernstein HM, Allen KN, Imperiali B, Straub JE J Biol Chem. 2023 Oct;299(10):105194. doi: 10.1016/j.jbc.2023.105194. Epub 2023 , Aug 25. PMID:37633332[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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