8e37 | pdb_00008e37

Structure of Campylobacter concisus wild-type SeMet PglC

spinqualitylabelsall models 8e37, resolution 3.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8e37 is a 8 chain structure with sequence from Campylobacter concisus 13826. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.01Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A7ZET4_CAMC1 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 (PGT) 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 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 undecaprenol phosphate with PGT 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 Aug 24:105194. doi: 10.1016/j.jbc.2023.105194. PMID:37633332 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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