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Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes

Pintacuda, Guido; Park, Ah Young; Keniry, Max; Dixon, Nicholas; Otting, Gottfried

Description

A novel nuclear magnetic resonance (NMR) strategy based on labeling with lanthanides achieves rapid determinations of accurate three-dimensional (3D) structures of protein-protein complexes. The method employs pseudocontact shifts (PCS) induced by a site-specifically bound lanthanide ion to anchor the coordinate system of the magnetic susceptibility tensor in the molecular frames of the two molecules. Simple superposition of the tensors detected in the two protein molecules brings them together...[Show more]

dc.contributor.authorPintacuda, Guido
dc.contributor.authorPark, Ah Young
dc.contributor.authorKeniry, Max
dc.contributor.authorDixon, Nicholas
dc.contributor.authorOtting, Gottfried
dc.date.accessioned2015-12-13T23:04:08Z
dc.identifier.issn0002-7863
dc.identifier.urihttp://hdl.handle.net/1885/85237
dc.description.abstractA novel nuclear magnetic resonance (NMR) strategy based on labeling with lanthanides achieves rapid determinations of accurate three-dimensional (3D) structures of protein-protein complexes. The method employs pseudocontact shifts (PCS) induced by a site-specifically bound lanthanide ion to anchor the coordinate system of the magnetic susceptibility tensor in the molecular frames of the two molecules. Simple superposition of the tensors detected in the two protein molecules brings them together in a 3D model of the protein-protein complex. The method is demonstrated with the 30 kDa complex between two subunits of Escherichia coli polymerase III, comprising the N-terminal domain of the exonuclease subunit e and the subunit θ. The 3D structures of the individual molecules were docked based on a limited number of PCS observed in 2D 15N-heteronuclear single quantum coherence spectra. Degeneracies in the mutual orientation of the protein structures were resolved by the use of two different lanthanide ions, Dy3+ and Er3+.
dc.publisherAmerican Chemical Society
dc.sourceJournal of the American Chemical Society
dc.subjectKeywords: Enzymes; Escherichia coli; Ions; Magnetic susceptibility; Mathematical models; Nuclear magnetic resonance; Proteins; Rare earth elements; Molecular frames; Protein-protein complexes; Quantum coherence; Three-dimensional (3D) structures; Complexation; erbi
dc.titleLanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume128
dc.date.issued2006
local.identifier.absfor060199 - Biochemistry and Cell Biology not elsewhere classified
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationMigratedxPub13530
local.type.statusPublished Version
local.contributor.affiliationPintacuda, Guido, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationPark, Ah Young, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationKeniry, Max, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationDixon, Nicholas, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOtting, Gottfried, College of Physical and Mathematical Sciences, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue11
local.bibliographicCitation.startpage3696
local.bibliographicCitation.lastpage3702
local.identifier.doi10.1021/ja057008z
dc.date.updated2015-12-12T07:53:44Z
local.identifier.scopusID2-s2.0-33645390370
CollectionsANU Research Publications

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