5E11

Second PDZ domain of Ligand of Numb protein X 2 by Laue crystallography (no electric field)

Summary for 5E11

• Entry DOI: 10.2210/pdb5e11/pdb
• Related: 2VWR 5E1Y 5E21 5E22
• Descriptor: Ligand of Numb protein X 2 (2 entities in total)
• Functional Keywords: unperturbed, off state., protein binding
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 10310.74

Authors

Hekstra, D.R.,White, K.I.,Socolich, M.A.,Henning, R.W.,Srajer, V.,Ranganathan, R. (deposition date: 2015-09-29, release date: 2016-12-07, Last modification date: 2024-03-06)

Primary citation

Hekstra, D.R.,White, K.I.,Socolich, M.A.,Henning, R.W.,Srajer, V.,Ranganathan, R.
Electric-field-stimulated protein mechanics.
Nature, 540:400-405, 2016

PubMed Abstract: The internal mechanics of proteins-the coordinated motions of amino acids and the pattern of forces constraining these motions-connects protein structure to function. Here we describe a new method combining the application of strong electric field pulses to protein crystals with time-resolved X-ray crystallography to observe conformational changes in spatial and temporal detail. Using a human PDZ domain (LNX2) as a model system, we show that protein crystals tolerate electric field pulses strong enough to drive concerted motions on the sub-microsecond timescale. The induced motions are subtle, involve diverse physical mechanisms, and occur throughout the protein structure. The global pattern of electric-field-induced motions is consistent with both local and allosteric conformational changes naturally induced by ligand binding, including at conserved functional sites in the PDZ domain family. This work lays the foundation for comprehensive experimental study of the mechanical basis of protein function.

PubMed: 27926732
DOI: 10.1038/nature20571

Experimental method

X-RAY DIFFRACTION (1.8 Å)