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. 2003 Mar;121(3):227–244. doi: 10.1085/jgp.20028768

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Copyright © 2003, The Rockefeller University Press

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Figure 1. — Sequence analysis of conserved COOH-terminal regions of MscL and comparison with the cartilage protein COMP. Alignment of S3 domains (residues 118–132 for EcoMscL) for 19 representative MscL homologues from different bacterial species, the consensus and the sequence of the third heptad of the oligomerization domain of COMP (A). The fragment of the crystal structure of COMP representing the aligned sequence (green box), which shows all hydrophobic side chains packed inside the fivefold coiled-coil and the salt bridges between R48 or R52 (blue) and D46 (red) on different chains (B). Helical wheel representations of the packing of helices in the crystal structure of TbMscL (C) and in EcoMscL modeled after COMP (D).