E. coli trp repressor forms a domain-swapped array in aqueous alcohol

Catherine L. Lawson; Brian Benoff; Tatyana Berger; Helen M. Berman; Jannette Carey

doi:10.1016/j.str.2004.03.019

E. coli trp repressor forms a domain-swapped array in aqueous alcohol

Catherine L. Lawson, Brian Benoff, Tatyana Berger, Helen M. Berman, Jannette Carey

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 Å X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.

Original language	English (US)
Pages (from-to)	1099-1108
Number of pages	10
Journal	Structure
Volume	12
Issue number	6
DOIs	https://doi.org/10.1016/j.str.2004.03.019
State	Published - Jun 2004

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

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10.1016/j.str.2004.03.019

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@article{9017fc29359245848de72be8065fe2a4,

title = "E. coli trp repressor forms a domain-swapped array in aqueous alcohol",

abstract = "The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 {\AA} X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.",

author = "Lawson, {Catherine L.} and Brian Benoff and Tatyana Berger and Berman, {Helen M.} and Jannette Carey",

note = "Funding Information: We are grateful to Andy Napoli, Mike Becker, Dieter Schneider, and Bob Sweet for assistance at BNL-NSLS beamlines X25 and X12B, to Valerie Copi{\'e} and Rob Tyler for wild-type trpR used in the SAXS study, to Lizhu Liu for assistance at beamline X27C, and to Ben Hsaio, Lizhi Liu, and Dieter Schneider for guidance in interpretation of the SAXS data. This work was supported by NIH GM21589 to H.M.B. and C.L.L. and NSF MCB01-36094 to J.C. ",

year = "2004",

month = jun,

doi = "10.1016/j.str.2004.03.019",

language = "English (US)",

volume = "12",

pages = "1099--1108",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "6",

}

TY - JOUR

T1 - E. coli trp repressor forms a domain-swapped array in aqueous alcohol

AU - Lawson, Catherine L.

AU - Benoff, Brian

AU - Berger, Tatyana

AU - Berman, Helen M.

AU - Carey, Jannette

N1 - Funding Information: We are grateful to Andy Napoli, Mike Becker, Dieter Schneider, and Bob Sweet for assistance at BNL-NSLS beamlines X25 and X12B, to Valerie Copié and Rob Tyler for wild-type trpR used in the SAXS study, to Lizhu Liu for assistance at beamline X27C, and to Ben Hsaio, Lizhi Liu, and Dieter Schneider for guidance in interpretation of the SAXS data. This work was supported by NIH GM21589 to H.M.B. and C.L.L. and NSF MCB01-36094 to J.C.

PY - 2004/6

Y1 - 2004/6

N2 - The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 Å X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.

AB - The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 Å X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.

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U2 - 10.1016/j.str.2004.03.019

DO - 10.1016/j.str.2004.03.019

M3 - Article

C2 - 15274929

AN - SCOPUS:2942587506

SN - 0969-2126

VL - 12

SP - 1099

EP - 1108

JO - Structure

JF - Structure

IS - 6

ER -

E. coli trp repressor forms a domain-swapped array in aqueous alcohol

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