4n9w
From Proteopedia
Crystal structure of phosphatidyl mannosyltransferase PimA
Structural highlights
Function[PIMA_MYCS2] Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 2 of a phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositola of PIM1.[1] [2] Publication Abstract from PubMedSecondary 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 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. Secondary structure reshuffling modulates glycosyltransferase function at the membrane.,Giganti D, Albesa-Jove D, Urresti S, Rodrigo-Unzueta A, Martinez MA, Comino N, Barilone N, Bellinzoni M, Chenal A, Guerin ME, Alzari PM Nat Chem Biol. 2015 Jan;11(1):16-8. doi: 10.1038/nchembio.1694. Epub 2014 Nov 17. PMID:25402770[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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