7jnf | pdb_00007jnf

The structure of CBM32-1 and CBM32-2 domains from Clostridium perfringens ZmpB in complex with GalNAc

spinqualitylabelsall models 7jnf, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7jnf is a 1 chain structure with sequence from Clostridium perfringens ATCC 13124. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: A2G, CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2YN38_CLOP1 Publication Abstract from PubMed A challenge faced by peptidases is the recognition of highly diverse substrates. A feature of some peptidase families is the capacity to specifically use post-translationally added glycans present on their protein substrates as a recognition determinant. This is ultimately critical to enabling peptide bond hydrolysis. This class of enzyme is also frequently large and architecturally sophisticated. However, the molecular details underpinning glycan recognition by these O-glycopeptidases, the importance of these interactions, and the functional roles of their ancillary domains remain unclear. Here, using the Clostridium perfringens ZmpA, ZmpB, and ZmpC M60 peptidases as model proteins, we provide structural and functional insight into how these intricate proteins recognize glycans as part of catalytic and noncatalytic substrate recognition. Structural, kinetic, and mutagenic analyses support the key role of glycan recognition within the M60 domain catalytic site, though they point to ZmpA as an apparently inactive enzyme. Wider examination of the Zmp domain content reveals noncatalytic carbohydrate binding as a feature of these proteins. The complete three-dimensional structure of ZmpB provides rare insight into the overall molecular organization of a highly multimodular enzyme and reveals how the interplay of individual domain function may influence biological activity. O-glycopeptidases frequently occur in host-adapted microbes that inhabit or attack mucus layers. Therefore, we anticipate that these results will be fundamental to informing more detailed models of how the glycoproteins that are abundant in mucus are destroyed as part of pathogenic processes or liberated as energy sources during normal commensal lifestyles. Architecturally complex O-glycopeptidases are customized for mucin recognition and hydrolysis.,Pluvinage B, Ficko-Blean E, Noach I, Stuart C, Thompson N, McClure H, Buenbrazo N, Wakarchuk W, Boraston AB Proc Natl Acad Sci U S A. 2021 Mar 9;118(10). pii: 2019220118. doi:, 10.1073/pnas.2019220118. PMID:33658366 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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