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Human PRPS1 filaments stabilize allosteric sites to regulate activity

Human PRPS1 filaments stabilize allosteric sites to regulate activity

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10033377

Human PRPS1 filaments stabilize allosteric sites to regulate activity

About this item

Full title

Human PRPS1 filaments stabilize allosteric sites to regulate activity

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2023-03, Vol.30 (3), p.391-402

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

The universally conserved enzyme phosphoribosyl pyrophosphate synthetase (PRPS) assembles filaments in evolutionarily diverse organisms. PRPS is a key regulator of nucleotide metabolism, and mutations in the human enzyme PRPS1 lead to a spectrum of diseases. Here we determine structures of human PRPS1 filaments in active and inhibited states, with...

Alternative Titles

Full title

Human PRPS1 filaments stabilize allosteric sites to regulate activity

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10033377

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10033377

Other Identifiers

ISSN

1545-9993,1545-9985

E-ISSN

1545-9985

DOI

10.1038/s41594-023-00921-z

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