Literature summary extracted from

Giganti, D.; Albesa-Jove, D.; Urresti, S.; Rodrigo-Unzueta, A.; Martinez, M.A.; Comino, N.; Barilone, N.; Bellinzoni, M.; Chenal, A.; Guerin, M.E.; Alzari, P.M.
Secondary structure reshuffling modulates glycosyltransferase function at the membrane (2015), Nat. Chem. Biol., 11, 16-18.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.4.1.345	crystal structures of PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including beta-strand-to-alpha-helix and alpha-helix-to-beta-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane	Mycolicibacterium smegmatis

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.4.1.345	W82F W349F	the environment of at least one of the two tryptophan residues (Trp82 and/or Trp349) undergoes structural changes in the presence of membranes	Mycolicibacterium smegmatis

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.1.345	Mycolicibacterium smegmatis	A0QWG6	-	-
2.4.1.345	Mycolicibacterium smegmatis ATCC 700084	A0QWG6	-	-

General Information

EC Number	General Information	Comment	Organism
2.4.1.345	metabolism	PimA undergoes a conformational reorganization of its N-terminal domain upon phosphatidylinositol membrane interaction.The presence of anionic phospholipids increases the susceptibility of PimA to proteolysis	Mycolicibacterium smegmatis

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Release 2023.1 (January 2023)