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PLOD3
Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia
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Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 is an enzyme that in humans is encoded by the PLOD3 gene.[5][6][7]
The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity.[7]
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Structure and functions
Cryo-electron microscopy (Cryo-EM) study has revealed the structural architecture of PLOD3 within the lysyl O-linked glycosylation complex (KOGG complex), which plays a crucial role in procollagen maturation. [8]
The KOGG complex consists of a PLOD3 (LH3) dimer, a Procollagen galactosyltransferase 1 (ColGalT1) dimer, and UDP-bound cofactors, orchestrating the hydroxylation (by PLOD3) and dual glycosylation (galactosylation by ColGalT1 and glucosylation by PLOD3) of lysine residues in the endoplasmic reticulum (ER) lumen. These modifications are essential for collagen cross-linking, fibrillogenesis, and overall structural integrity.
Additionally, the structural study suggests that the KOGG complex can polymerize into a larger, fiber-like enzyme supercomplex, which may further regulate collagen modification and assembly. Defects in PLOD3 function or glycosylation efficiency have been implicated in connective tissue disorders, including osteogenesis imperfecta and fibrosis-related diseases.
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References
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