PDBsum entry 5e11

Protein binding

PDB id: 5e11

Contents

Protein chain

95 a.a.

Waters ×100

PDB id:

5e11

Name:

Protein binding

Title:

Second pdz domain of ligand of numb protein x 2 by laue crystallography (no electric field)

Structure:

Ligand of numb protein x 2. Chain: 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

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: lnx2, pdzrn1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.80Å R-factor: 0.133 R-free: 0.148

Authors:

D.R.Hekstra,K.I.White,M.A.Socolich,R.W.Henning,V.Srajer,R.Ranganathan

Key ref:

D.R.Hekstra et al. (2016). Electric-field-stimulated protein mechanics. Nature, 540, 400-405. PubMed id: 27926732

Date:

29-Sep-15 Release date: 07-Dec-16

Protein chain

Q8N448  (LNX2_HUMAN) -  Ligand of Numb protein X 2 from Homo sapiens

Seq: 690 a.a.

Struc: 95 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

Nature 540:400-405 (2016)

PubMed id: 27926732

Electric-field-stimulated protein mechanics.

D.R.Hekstra, K.I.White, M.A.Socolich, R.W.Henning, V.Šrajer, R.Ranganathan.

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^PDZ2) 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.