Analysis of the Differences between the Two Domains of Myosin Essential Light Chain




A comparison of the conformations of the N- and C-terminal domains of myosin essential light chain: Interhelical distance difference matrix (DDM) entries are shown in the left panels and interhelical contacts in the two domains of ELC are shown in the center (ELC-N) and right (ELC-C) panels. The DDM entries are mapped onto a ribbon representation of ELC-N. Residues that are moderately closer together in ELC-N (DD between -2 and -5 angstroms) are connected by light blue lines. Residues that are much closer together in ELC-N (DD less than -5 angstroms) are connected by dark blue lines. Residues that are moderately closer together in ELC-C (DD between 2 and 5 angstroms) are connected by pink lines. Residues that are much closer together in ELC-C (DD greater than 5 angstroms) are connected by red lines. Interhelical contacts are categorized on the basis of the centers of geometry (CG) of the respective residues. Close contacts (distance between CGs less than 5 angstroms) are shown as purple lines, mid-range contacts (distance between CGs between 5 andf 6.5 angstroms) are shown as blue lines, and long-range contacts (distance between CGs between 6.5 and 8 angstroms) are shown as green lines. Contacts unique to one domain are shown as solid lines. Contacts found in both domains are shownas dotted lines. The helices were rendered as ribbons using InsightII (MSI, San Diego, CA), and the DDs and contacts were rendered as distance restraints using the NMR_Refine module of InsightII. The coordinates are from PDB entry 1WDC.

This graphic was figure 3 in the paper:
Nelson, M.R., W.J. Chazin. An Interaction-Based Analysis of Calcium-Induced Conformational Changes in Ca2+ Sensor Proteins (1998) Prot. Sci. 7, 270-282.


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