期刊
BIOCHEMISTRY
卷 46, 期 49, 页码 13975-13982出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi701210j
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资金
- Intramural NIH HHS Funding Source: Medline
- NCI NIH HHS [NC01-CO-12400] Funding Source: Medline
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 angstrom. Upon refinement against H-alpha-C-alpha, H-N-N, and C-alpha-C' J-modulated residual dipolar couplings, the backbone rmsd improves to 0.22 angstrom. 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 suprastructuting by substituting for an H-NS dimer.
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