Supplementary information
From the following article:
Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products
Tomohisa Kuzuyama, Joseph P. Noel and Stéphane B. Richard
Nature 435, 983-987 (16 June 2005)
doi:10.1038/nature03668
Supplementary Table S1
This summarizes an upstream region of the gene cluster containing the MVA pathway genes revealing three new open reading frames or orfs designated orf1, orf2, and orf3. The comparative analysis of these orfs with genes encoding functionally characterized proteins is also summarized.
Supplementary Table S2
This summarizes the statistics for the x-ray structure determination of Orf2 and the refinement of several small molecule complexes with Orf2.
Supplementary Discussion
This includes additional information and discussion pertaining to large family of structurally diverse proteins displaying barrel folds. In addition, further discussion of the possible mechanisms accompanying prenyl group transfer to aromatic small molecules is discussed.
Supplementary Figure S1
This illustrates the structure-based multiple sequence alignment of Orf2 and three other bacterial proteins belonging to the Orf2 family of aromatic PTases. The secondary structure shown is based on the experimentally determined x-ray structure of Orf2.
Supplementary Figure S2
This summarizes the comparison of protein barrel fold categories. Both topology diagrams illustrating and contrasting the connectivity of secondary structure elements as well as ribbon diagrams in two orthogonal orientations are shown.
Supplementary Figure S3
This depicts the proposed electrophilic mechanism used by Orf2 for aromatic small molecule prenylation. Both schematic and realistic views are shown and discussed in depth in the Supplementary Discussion.
Supplementary Figure S4
This illustrates the comparative modeling of CloQ/NovQ and HypSc, two other bacterial PTases belonging to the Orf2 structural family of PT-barrels.
Supplementary Data
The 1NMR and MS data used to determine the chemical identity of several prenylated products produced by Orf2 using in vitro incubations.
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