The high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS.

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TitleThe high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS.
Publication TypeJournal Article
Year of Publication2007
AuthorsMcFeeters, RL, Altieri, AS, Cherry, S, Tropea, JE, Waugh, DS, R Byrd, A
JournalBiochemistry
Volume46
Issue49
Pagination13975-82
Date Published2007 Dec 11
ISSN0006-2960
KeywordsAmino Acid Sequence, Bacterial Proteins, DNA-Binding Proteins, Escherichia coli Proteins, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, Yersinia enterocolitica
Abstract

The high-resolution solution structure of Yersinia modulating protein YmoA is presented. The protein is all helical with the first three of four helices forming the central core. Structures calculated with only NOE and dihedral restraints exhibit a backbone root-mean-square deviation (rmsd) of 0.77 A. Upon refinement against Halpha-Calpha, HN-N, and Calpha-C' J-modulated residual dipolar couplings, the backbone rmsd improves to 0.22 A. YmoA has a high amino acid sequence identity to and a similar overall fold to Escherichia coli hemolysin expression modulating protein Hha; however, structural differences do occur. YmoA is also found to be structurally similar to the histone-like nucleoid structuring protein H-NS, indicating that YmoA may intercalate into higher-order H-NS suprastructuring by substituting for an H-NS dimer.

DOI10.1021/bi701210j
Alternate JournalBiochemistry
PubMed ID18001134
Grant ListNC01-CO-12400 / CO / NCI NIH HHS / United States
/ / Intramural NIH HHS / United States