Secondary structure reshuffling modulates glycosyltransferase function at the membrane.
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.
1] Institut Pasteur, Unité de Microbiologie Structurale, CNRS UMR 3528, Paris, France. [2] Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain. [3] Departamento de Bioquímica, Universidad del País Vasco, Spain.
David
D
Giganti
1] Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain. [2] Departamento de Bioquímica, Universidad del País Vasco, Spain.
David
D
Albesa-Jové
1] Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain. [2] Departamento de Bioquímica, Universidad del País Vasco, Spain.
Saioa
S
Urresti
1] Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain. [2] Departamento de Bioquímica, Universidad del País Vasco, Spain.
Ane
A
Rodrigo-Unzueta
Institut Pasteur, Unité de Microbiologie Structurale, CNRS UMR 3528, Paris, France.
Mariano A
MA
Martínez
1] Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain. [2] Departamento de Bioquímica, Universidad del País Vasco, Spain.
Natalia
N
Comino
Institut Pasteur, Unité de Microbiologie Structurale, CNRS UMR 3528, Paris, France.
Nathalie
N
Barilone
Institut Pasteur, Unité de Microbiologie Structurale, CNRS UMR 3528, Paris, France.
Marco
M
Bellinzoni
Institut Pasteur, Unité de Biochimie des Interactions Macromoléculaires, CNRS UMR 3528, Paris, France.
Alexandre
0000000249591003
A
Chenal
1] Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain. [2] Departamento de Bioquímica, Universidad del País Vasco, Spain. [3] IKERBASQUE, Basque Foundation for Science, Bilbao, Spain.
Marcelo E
ME
Guerin
Institut Pasteur, Unité de Microbiologie Structurale, CNRS UMR 3528, Paris, France.
Pedro M
PM
Alzari
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism*; D018360:Crystallography, X-Ray; D016695:Glycosyltransferases / Q000378:metabolism*; D006801:Humans; D008364:Mannosyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010743:Phospholipids / Q000378:metabolism; D017433:Protein Structure, Secondary / Q000235:genetics
D001426:Bacterial Proteins; D010743:Phospholipids; D016695:Glycosyltransferases; D008364:Mannosyltransferases; C543796:phosphatidyl-myo-inositol mannosyltransferase PimA, Mycobacterium smegmatis