Next Article in Journal
A Rare De Novo RAI1 Gene Mutation Affecting BDNF-Enhancer-Driven Transcription Activity Associated with Autism and Atypical Smith-Magenis Syndrome Presentation
Previous Article in Journal
Expression of a Synthetic Gene for the Major Cytotoxin (Cyt1Aa) of Bacillus thuringiensis subsp. israelensis in the Chloroplast of Wild-Type Chlamydomonas
Article Menu

Export Article

Open AccessArticle
Biology 2018, 7(2), 30; https://doi.org/10.3390/biology7020030

Open Conformation of the Escherichia coli Periplasmic Murein Tripeptide Binding Protein, MppA, at High Resolution

Department of Biological Sciences, MC567, University of Illinois, 900 S. Ashland Ave, Chicago, IL 60607, USA
*
Author to whom correspondence should be addressed.
Received: 23 March 2018 / Revised: 11 May 2018 / Accepted: 11 May 2018 / Published: 19 May 2018
Full-Text   |   PDF [881 KB, uploaded 19 May 2018]   |  

Abstract

Periplasmic ligand-binding proteins (PBPs) bind ligands with a high affinity and specificity. They undergo a large conformational change upon ligand binding, and they have a robust protein fold. These physical features have made them ideal candidates for use in protein engineering projects to develop novel biosensors and signaling molecules. The Escherichia coli MppA (murein peptide permease A) PBP binds the murein tripeptide, l-alanyl-γ-d-glutamyl-meso-diaminopimelate, (l-Ala-γ-d-Glu-meso-Dap), which contains both a D-amino acid and a gamma linkage between two of the amino acids. We have solved a high-resolution X-ray crystal structure of E. coli MppA at 1.5 Å resolution in the unliganded, open conformation. Now, structures are available for this member of the PBP protein family in both the liganded/closed form and the unliganded/open form. View Full-Text
Keywords: periplasmic ligand-binding protein; murein tripeptide; murein recycling; ligand binding; transmembrane transport periplasmic ligand-binding protein; murein tripeptide; murein recycling; ligand binding; transmembrane transport
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

SciFeed

Share & Cite This Article

MDPI and ACS Style

Bhatt, F.; Patel, V.; Jeffery, C.J. Open Conformation of the Escherichia coli Periplasmic Murein Tripeptide Binding Protein, MppA, at High Resolution. Biology 2018, 7, 30.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biology EISSN 2079-7737 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top