1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function

Julien Boudet; Anne Chouquet; Aicha Chahboune; Cécile Giustini; Bernard Joris; Jean-Pierre Simorre; Catherine Bougault

doi:10.1007/s12104-007-9025-0

1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function

Biomol NMR Assign. 2007 Jul;1(1):89-91. doi: 10.1007/s12104-007-9025-0. Epub 2007 Jul 7.

Authors

Julien Boudet¹, Anne Chouquet, Aicha Chahboune, Cécile Giustini, Bernard Joris, Jean-Pierre Simorre, Catherine Bougault

Affiliation

¹ Laboratoire de Résonance Magnétique Nucléaire, CEA, CNRS, Université Joseph Fourier, Institut de Biologie Structurale Jean-Pierre Ebel, 41 Rue Jules Horowitz, 38027 Grenoble, France.

PMID: 19636835
DOI: 10.1007/s12104-007-9025-0

Abstract

The ampG gene codes for a permease required to uptake anhydro-muropeptides into bacterial cytoplasm. Located upstream in the same operon, is another 579-base-pair-long open reading frame encoding a putative lipoprotein YajG, whose nearly complete 1H,13C,15N assignments are reported here.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Base Sequence
DNA Primers / genetics
DNA, Bacterial / genetics
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / genetics
Lipoproteins / chemistry
Lipoproteins / genetics
Molecular Structure
Nuclear Magnetic Resonance, Biomolecular
Recombinant Proteins / chemistry
Recombinant Proteins / genetics

Substances

DNA Primers
DNA, Bacterial
Escherichia coli Proteins
Lipoproteins
Recombinant Proteins