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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Cell Membrane / enzymology
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Cell Membrane / metabolism*
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Crystallography, X-Ray
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Glycosyltransferases / metabolism*
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Humans
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Mannosyltransferases / chemistry*
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Mannosyltransferases / genetics
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Mannosyltransferases / isolation & purification
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Models, Molecular
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Mutagenesis, Site-Directed
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Phospholipids / metabolism
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Protein Structure, Secondary* / genetics
Substances
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Bacterial Proteins
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Phospholipids
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Glycosyltransferases
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Mannosyltransferases
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phosphatidyl-myo-inositol mannosyltransferase PimA, Mycobacterium smegmatis