Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR

PDF Version Also Available for Download.

Description

The chemical shift of the {sup 129}Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins (Rubin et al. 2000; Lowery et al. 2004). Here we show that the {sup 129}Xe shift can sense more subtle changes: magnesium binding, BeF{sub 3}{sup -} activation, and peptide binding by the E. coli chemotaxis Y protein. {sup 1}H-{sup 15}N correlation spectroscopy and x-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift ... continued below

Physical Description

27 pages

Creation Information

Lowery, Thomas J.; Doucleff, Michealeen; Ruiz, E. Janette; Rubin, Seth M.; Pines, Alexander & Wemmer, David E. February 1, 2005.

Context

This article is part of the collection entitled: Office of Scientific & Technical Information Technical Reports and was provided by UNT Libraries Government Documents Department to Digital Library, a digital repository hosted by the UNT Libraries. More information about this article can be viewed below.

Who

People and organizations associated with either the creation of this article or its content.

Provided By

UNT Libraries Government Documents Department

Serving as both a federal and a state depository library, the UNT Libraries Government Documents Department maintains millions of items in a variety of formats. The department is a member of the FDLP Content Partnerships Program and an Affiliated Archive of the National Archives.

Contact Us

What

Descriptive information to help identify this article. Follow the links below to find similar items on the Digital Library.

Description

The chemical shift of the {sup 129}Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins (Rubin et al. 2000; Lowery et al. 2004). Here we show that the {sup 129}Xe shift can sense more subtle changes: magnesium binding, BeF{sub 3}{sup -} activation, and peptide binding by the E. coli chemotaxis Y protein. {sup 1}H-{sup 15}N correlation spectroscopy and x-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site.

Physical Description

27 pages

Notes

OSTI as DE00841325

Source

  • Journal Name: Protein Science; Journal Volume: 14; Journal Issue: 4; Other Information: Submitted to Protein Science: Volume 14, No.4; Journal Publication Date: 04/2005

Language

Item Type

Identifier

Unique identifying numbers for this article in the Digital Library or other systems.

  • Report No.: LBNL--56980
  • Grant Number: AC03-76SF00098
  • DOI: 10.1110/ps.041231005 | External Link
  • Office of Scientific & Technical Information Report Number: 841325
  • Archival Resource Key: ark:/67531/metadc781200

Collections

This article is part of the following collection of related materials.

Office of Scientific & Technical Information Technical Reports

Reports, articles and other documents harvested from the Office of Scientific and Technical Information.

Office of Scientific and Technical Information (OSTI) is the Department of Energy (DOE) office that collects, preserves, and disseminates DOE-sponsored research and development (R&D) results that are the outcomes of R&D projects or other funded activities at DOE labs and facilities nationwide and grantees at universities and other institutions.

What responsibilities do I have when using this article?

When

Dates and time periods associated with this article.

Creation Date

  • February 1, 2005

Added to The UNT Digital Library

  • Dec. 3, 2015, 9:30 a.m.

Description Last Updated

  • April 4, 2016, 12:42 p.m.

Usage Statistics

When was this article last used?

Yesterday: 0
Past 30 days: 0
Total Uses: 2

Interact With This Article

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

International Image Interoperability Framework

IIF Logo

We support the IIIF Presentation API

Lowery, Thomas J.; Doucleff, Michealeen; Ruiz, E. Janette; Rubin, Seth M.; Pines, Alexander & Wemmer, David E. Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR, article, February 1, 2005; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc781200/: accessed September 20, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.