Journal: Biochemistry

Article Title: Biochemical and spectroscopic characterization of a radical SAM enzyme involved in the formation of a peptide thioether crosslink

doi: 10.1021/acs.biochem.6b00145

Figure Lengend Snippet: (A) The mature nisin peptide has thioether crosslinks between Cys and dehydroalanine (Dha) and dehydrobutyrine (Dhb) residues. (B) The sactipeptide subtilosin A is shown, highlighting the three thioether crosslinks. In its fully mature form, subtilosin A is circularized. The stereochemistry at the three attachment sites is shown in red. The sactipeptides are distinct from the lanthipeptides in that the thioether crosslinks are formed to the Cα of the peptide. (C) Sequence logo for the SCIFF peptides showing the conserved C-terminal sequence. The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal Omega61 multiple sequence alignment and visualized by Weblogo.62,63

Article Snippet: The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal Omega61 multiple sequence alignment and visualized by Weblogo.62,63.

Techniques: Sequencing, Generated

Journal: The Journal of Biological Chemistry

Article Title: Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments *

doi: 10.1074/jbc.M110.148684

Figure Lengend Snippet: Cardiac TnT contains a highly conserved PKA docking site. A, schematic illustration shows the location of the PKA binding site and cardiac-specific cTnI-Ser23-Ser24 phosphorylation sites (star). Drawing of the troponin complex is based on the crystal structure of the troponin core domain (50). N-terminal region of cTnT (residues 1–204) was not solved in the crystal structure. Rectangles represent helical structures. cTnC is colored red, cTnI is green, and cTnT is blue. B, ClustalW multiple sequence alignment of cTnT with nine other AKAPs. Conserved residues responsible for tethering PKA are shown in white. The high homology between cTnT and Ht31 is also shown (boxed). C, surface representation of cTnT (PDB 1J1D) helix 203–224 shows the position of hydrophobic residues (red) involved in PKA docking.

Article Snippet: In silico analysis of the cTnT amino acid sequence using the ClustalW multiple alignment algorithm (part of the MacVector 11 sequence analysis suite) identified a fragment of an amphipathic α-helix (spanning residues 212–224) as a putative PKA-R binding site ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window FIGURE 2. caption a7 Cardiac TnT contains a highly conserved PKA docking site.

Techniques: Binding Assay, Phospho-proteomics, Sequencing