SEARCH

SEARCH BY CITATION

Additional Supporting Information may be found in the online version of this article.

FilenameFormatSizeDescription
pro2262-sup-0001-suppinfo.tiff3007KSupplementary Figure 1. Comparison of apo (monomeric) and holo (dimeric) SaBPL. The cartoon representation of the dimer is coloured according to the similarity of the apo and holo SaBPL structures. Blue indicates that the structures are similar ie. the RMSD Cα atoms is less 2 Å. The colour is ramped through to red where the RMSD Cα is greater than 4 Å.
pro2262-sup-0002-suppinfo.tiff3249KSupplementary Figure 2. Interaction of holo-SaBPL with the S. aureus bioO (Sa-bioO) DNA sequence. A) Electrophoretic mobility shift assay (EMSA) demonstrating that holo-SaBPL binds to the Sa-bioO DNA sequence but not to an unrelated dsDNA sequence. Lane 1: 0 μM Btyl-SaBPL+ 0.29 μM Sa-bioO; Lane 2: 0.29 μM Btyl-SaBPL+ 0.29 μM Sa-bioO; Lane 3: 0 μM Btyl-SaBPL+ 0.292 μM control non specific DNA; Lane 5: 0.29 μM Btyl-SaBPL + 0.292 μM control DNA. B) The region of the Staphylococcus aureus genome identified as Sa-bioO. Dashes are used to indicate the regions of the sequence that represent an inverted repeat and the bolded/boxed bases are the predicted regions of the sequence recognised by SaBPL.
pro2262-sup-0003-suppinfo.tiff2756KSupplementary Figure 3. Model of the SaBPL/BCCP complex. Cartoon representation of the SaBCCP structure (PDB ID: 3BG5; coloured in yellow) positioned against one monomer of the SaBPL dimer by analogy to the BPL/BCCP complex from P. horikoshii (PDB ID: 2EJG). This required that the C-terminal cap (coloured light pink) be slightly repositioned to avoid clashes. BCCP interacts at the BPL homodimer interface, as seen from its overlap with the second SaBPL monomer (purple). Its reactive site lysine is positioned just above the BBL (dark pink) at the reactive site where biotin is transferred.
pro2262-sup-0004-suppinfo.tiff2965KSupplementary Figure 4. Comparison of SaBPL dimer with EcBPL. SaBPL (top) and EcBPL (bottom: PDB ID: 1HXD) dimer structures are shown in cartoon representation. The SaBPL dimer interface differs from that of EcBPL resulting in a different angle of interaction of the catalytic domains (coloured green). Resultantly, the DNA binding domains (coloured light blue) are positioned differently in each model such that the α-helix 2 that binds at the major groove of target dsDNA are juxtaposed quite differently in the two models.
pro2262-sup-0005-suppinfo.tiff4274KSupplementary Figure 5. SAXS analysis of apo- and holo-SaBPL, SaBPL/DNA and SaBPL/BCCP. Enlarged versions of the ab initio reconstruction of the six samples overlaid with models derived from crystallographic structural data and modelling as described in Figure 3.
pro2262-sup-0006-suppinfo.tiff3623KSupplementary Figure 5. SAXS analysis of apo- and holo-SaBPL, SaBPL/DNA and SaBPL/BCCP. Enlarged versions of the ab initio reconstruction of the six samples overlaid with models derived from crystallographic structural data and modelling as described in Figure 3.
pro2262-sup-0007-suppinfo.doc80KSupporting Information

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.