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PDBsum entry 5e22
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Protein binding
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PDB id
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5e22
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PDB id:
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| Name: |
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Protein binding
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Title:
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The second pdz domain of ligand of numb protein x 2 in the presence of an electric field of ~1 mv/cm along the crystallographic x axis, with eightfold extrapolation of structure factor differences.
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Structure:
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Ligand of numb protein x 2. Chain: b, a. Fragment: second pdz domain (unp residues 336-424). Synonym: numb-binding protein 2,pdz domain-containing ring finger protein 1. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: lnx2, pdzrn1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.80Å
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R-factor:
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0.291
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R-free:
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0.313
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Authors:
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D.R.Hekstra,K.I.White,M.A.Socolich,R.W.Henning,V.Srajer,R.Ranganathan
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Key ref:
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D.R.Hekstra
et al.
(2016).
Electric-field-stimulated protein mechanics.
Nature,
540,
400-405.
PubMed id:
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Date:
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30-Sep-15
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Release date:
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07-Dec-16
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PROCHECK
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Headers
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References
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Q8N448
(LNX2_HUMAN) -
Ligand of Numb protein X 2 from Homo sapiens
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Seq:
Struc:
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690 a.a.
95 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 7 residue positions (black
crosses)
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Nature
540:400-405
(2016)
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PubMed id:
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Electric-field-stimulated protein mechanics.
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D.R.Hekstra,
K.I.White,
M.A.Socolich,
R.W.Henning,
V.Šrajer,
R.Ranganathan.
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ABSTRACT
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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 (LNX2PDZ2) 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.
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Links
