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. 2012 Oct 4;8(10):e1002958. doi: 10.1371/journal.ppat.1002958

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© 2012 Le et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Exploded view of the TED-MG8 interface, the MG8 domain (yellow) has been rotated 90° with respect to the TED (green). The thioester bond is shown as VDW spheres, variable residues within the pre-α4 loop, catalytic loop and MG8 interface (pink) are shown as sticks. Sequence alignments for TEP1 alleles in each variable region are illustrated by superposition of TEP1*S1 (pink) and TEP1*R1 (magenta) structures in panels (B–D) with non-variable regions colored by domain for both alleles. (B) The catalytic loop (966–976); TEP1*S1 Glu 966 is directed towards Ser 921 in place of TEP1*R1 Tyr 971, causing a 2 Å displacement of residues 967–979. (C) The pre-α4 loop (914–920); TEP1*S1 Gly 919 is directed towards Val 914 whereas TEP1*R1 Asn 919 is directed towards the solvent, (3.9 Å displacement of C_α). (D) Complementary variation within the MG8 domain; TEP1*S1 Asn 1260 is within hydrogen bonding distance of Gly 858 but TEP1*R1 Lys 1260 also interacts with Tyr 884, and TEP1*S1 Tyr 1275 is not compatible with hydrogen bonding to Trp 915 as is the case for TEP1*R1 Asn 1275.