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

Bhatt, Forum; Patel, Vishal; Jeffery, Constance

doi:10.3390/biology7020030

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

Journal Article · Sat May 19 00:00:00 EDT 2018 · Biology

DOI:https://doi.org/10.3390/biology7020030· OSTI ID:1628311

Bhatt, Forum ^[1]; Patel, Vishal ^[2]; Jeffery, Constance ^[2]

Univ. of Illinois, Chicago, IL (United States). Dept. of Biological Sciences; DOE/OSTI
Univ. of Illinois, Chicago, IL (United States). Dept. of Biological Sciences

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 Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1628311

Journal Information:: Biology, Journal Name: Biology Journal Issue: 2 Vol. 7; ISSN BBSIBX; ISSN 2079-7737

Publisher:: MDPICopyright Statement

Country of Publication:: United States

Language:: English

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