| Literature DB >> 25402770 |
David Giganti1, David Albesa-Jové2, Saioa Urresti2, Ane Rodrigo-Unzueta2, Mariano A Martínez3, Natalia Comino2, Nathalie Barilone3, Marco Bellinzoni3, Alexandre Chenal4, Marcelo E Guerin5, Pedro M Alzari3.
Abstract
Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand-to-α-helix and α-helix-to-β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.Entities:
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Year: 2014 PMID: 25402770 DOI: 10.1038/nchembio.1694
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040