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Article

Molecular basis of collagen galactosylation by GLT25D1.

Nature communications - 6 Feb 2026

Sun Huanhuan, Zhang Min, Shi Yunshu, Zhang Di, Hua Zhengkang, Yang Ping, Yang Yizheng, Li Jiameng, Chen Jiasheng, Wang Chao, Li Peifen, Hu Xinlin, Ke Yan, Zhang Mingjie, Liu Xiaotian, Yu Hongjun

Abstract excerpt

GLT25D1 O-galactosylates hydroxylysine residues in collagen and is essential for collagen maturation and function. Dysfunctions of GLT25D1 cause various tissue disorders. Despite its biological significance, the action mechanism of GLT25D1 remains enigmatic. Here we report the cryo-EM structures of human GLT25D1 and its ternary complex with UDP and hydroxylated acceptor substrates, revealing a bi-lobe...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 41651821
DOI: 10.1038/s41467-026-69234-1
PMCID: PMC12987934

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