Mining electron density for functionally relevant protein polysterism in crystal structures |
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Authors: | Email author" target="_blank">James?S?FraserEmail author Colin?J?Jackson |
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Institution: | (1) Department of Cellular and Molecular Pharmacology and California Institute of Quantitative Biosciences (QB3), University of California, San Francisco, San Francisco, CA 94158, USA;(2) Institut de Biologie Structurale, Rue Jules Horowitz, 38000 Grenoble, France;(3) Research School of Chemistry, Australian National University, Canberra, ACT, 0200, Australia |
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Abstract: | This review focuses on conceptual and methodological advances in our understanding and characterization of the conformational
heterogeneity of proteins. Focusing on X-ray crystallography, we describe how polysterism, the interconversion of pre-existing
conformational substates, has traditionally been analyzed by comparing independent crystal structures or multiple chains within
a single crystal asymmetric unit. In contrast, recent studies have focused on mining electron density maps to reveal previously
‘hidden’ minor conformational substates. Functional tests of the importance of minor states suggest that evolutionary selection
shapes the entire conformational landscape, including uniquely configured conformational substates, the relative distribution
of these substates, and the speed at which the protein can interconvert between them. An increased focus on polysterism may
shape the way protein structure and function is studied in the coming years. |
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Keywords: | |
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