8g1n | pdb_00008g1n

Structure of Campylobacter concisus PglC I57M/Q175M Variant with modeled C-terminus

spinqualitylabelsall models 8g1n, resolution 2.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8g1n is a 2 chain structure with sequence from Campylobacter concisus 13826. This structure supersedes the now removed PDB entry 5w7l. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.74Å Ligands: MG, PEF, PG4, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A7ZET4_CAMC1 Publication Abstract from PubMed Monotopic phosphoglycosyl transferases (monoPGTs) are an expansive superfamily of enzymes that catalyze the first membrane-committed step in the biosynthesis of bacterial glycoconjugates. MonoPGTs show a strong preference for their cognate nucleotide diphospho-sugar (NDP-sugar) substrates. However, despite extensive characterization of the monoPGT superfamily through previous development of a sequence similarity network comprising >38,000 nonredundant sequences, the connection between monoPGT sequence and NDP-sugar substrate specificity has remained elusive. In this work, we structurally characterize the C-terminus of a prototypic monoPGT for the first time and show that 19 C-terminal residues play a significant structural role in a subset of monoPGTs. This new structural information facilitated the identification of co-conserved sequence "fingerprints" that predict NDP-sugar substrate specificity for this subset of monoPGTs. A Hidden Markov model was generated that correctly assigned the substrate of previously unannotated monoPGTs. Together, these structural, sequence, and biochemical analyses have delivered new insight into the determinants guiding substrate specificity of monoPGTs and have provided a strategy for assigning the NDP-sugar substrate of a subset of enzymes in the superfamily that use UDP-di-N-acetyl bacillosamine. Moving forward, this approach may be applied to identify additional sequence motifs that serve as fingerprints for monoPGTs of differing UDP-sugar substrate specificity. Co-conserved sequence motifs are predictive of substrate specificity in a family of monotopic phosphoglycosyl transferases.,Anderson AJ, Dodge GJ, Allen KN, Imperiali B Protein Sci. 2023 Jun;32(6):e4646. doi: 10.1002/pro.4646. PMID:37096962 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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