pone.0286370.g001.tif (1.31 MB)

Structure comparison of MAP30 and Momordin.

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posted on 2023-06-29, 18:13 authored by Norman R. Watts, Elif Eren, Ira Palmer, Paul L. Huang, Philip Lin Huang, Robert H. Shoemaker, Sylvia Lee-Huang, Paul T. Wingfield

(A) MAP30 and (B) Momordin as viewed towards their respective active-sites, with key residues discussed in the text highlighted as follows: catalytic-site (green), Mn+2-binding site (yellow), and on the active-site-distal face, the ribosome-binding site (cyan) with the c11-P peptide-interacting Tyr residue (magenta). (C) Sequence alignment of MAP30 and Momordin with residues highlighted as above. Note that the structures for both MAP30 (PDB: 1D8V, 1CF5) and Momordin (PDB: 1MOM, 1AHA) are all missing 23 N-terminal residues. The C-terminal 19 residues are shown in the nuclear magnetic resonance structure of MAP30 (PDB: 1D8V) but not in the X-ray crystal structures of either protein. The N-terminal residues were missing, and C-terminal residues were present, on both proteins employed here.