skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Structure of the 'Escherichia Coli' Leucine-Responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly

Abstract

The structure of Escherichia coli leucine-responsive regulatory protein (Lrp) cocrystallized with a short duplex oligodeoxynucleotide reveals a novel quaternary assembly in which the protein octamer forms an open, linear array of four dimers. In contrast, structures of the Lrp homologs LrpA, LrpC and AsnC crystallized in the absence of DNA show that these proteins instead form highly symmetrical octamers in which the four dimers form a closed ring. Although the DNA is disordered within the Lrp crystal, comparative analyses suggest that the observed differences in quaternary state may arise from DNA interactions during crystallization. Interconversion of these conformations, possibly in response to DNA or leucine binding, provides an underlying mechanism to alter the relative spatial orientation of the DNA-binding domains. Breaking of the closed octamer symmetry may be a common essential step in the formation of active DNA complexes by all members of the Lrp/AsnC family of transcriptional regulatory proteins.

Authors:
;
Publication Date:
Research Org.:
Stanford Linear Accelerator Center (SLAC)
Sponsoring Org.:
USDOE
OSTI Identifier:
909822
Report Number(s):
SLAC-REPRINT-2007-072
Journal ID: ISSN 0022-2836; JMOBAK; TRN: US200723%%211
DOE Contract Number:  
AC02-76SF00515
Resource Type:
Journal Article
Journal Name:
J. Mol. Biol. 366:1589,2007
Additional Journal Information:
Journal Volume: 366; Journal ID: ISSN 0022-2836
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CRYSTALLIZATION; DIMERS; DNA; ESCHERICHIA COLI; LEUCINE; ORIENTATION; PROTEINS; SYMMETRY; Other,OTHER

Citation Formats

de los Rios, S, Perona, J J, and /UC, Santa Barbara. Structure of the 'Escherichia Coli' Leucine-Responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly. United States: N. p., 2007. Web. doi:10.1016/j.jmb.2006.12.032.
de los Rios, S, Perona, J J, & /UC, Santa Barbara. Structure of the 'Escherichia Coli' Leucine-Responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly. United States. https://doi.org/10.1016/j.jmb.2006.12.032
de los Rios, S, Perona, J J, and /UC, Santa Barbara. Mon . "Structure of the 'Escherichia Coli' Leucine-Responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly". United States. https://doi.org/10.1016/j.jmb.2006.12.032.
@article{osti_909822,
title = {Structure of the 'Escherichia Coli' Leucine-Responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly},
author = {de los Rios, S and Perona, J J and /UC, Santa Barbara},
abstractNote = {The structure of Escherichia coli leucine-responsive regulatory protein (Lrp) cocrystallized with a short duplex oligodeoxynucleotide reveals a novel quaternary assembly in which the protein octamer forms an open, linear array of four dimers. In contrast, structures of the Lrp homologs LrpA, LrpC and AsnC crystallized in the absence of DNA show that these proteins instead form highly symmetrical octamers in which the four dimers form a closed ring. Although the DNA is disordered within the Lrp crystal, comparative analyses suggest that the observed differences in quaternary state may arise from DNA interactions during crystallization. Interconversion of these conformations, possibly in response to DNA or leucine binding, provides an underlying mechanism to alter the relative spatial orientation of the DNA-binding domains. Breaking of the closed octamer symmetry may be a common essential step in the formation of active DNA complexes by all members of the Lrp/AsnC family of transcriptional regulatory proteins.},
doi = {10.1016/j.jmb.2006.12.032},
url = {https://www.osti.gov/biblio/909822}, journal = {J. Mol. Biol. 366:1589,2007},
issn = {0022-2836},
number = ,
volume = 366,
place = {United States},
year = {2007},
month = {7}
}