2k5s

YmoA

spinqualitylabelsall models 2k5s Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k5s is a 1 chain structure with sequence from Yersinia pestis. This structure supersedes the now removed PDB entry 2jvp. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YMOA_YERPE Modulates the thermoregulation of VirF, and hence the yop regulon, as well as the expression of the enterotoxin gene yst. It is supposed to be involved in chromosome structure and DNA topology; probably by means of compaction of DNA (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS.,McFeeters RL, Altieri AS, Cherry S, Tropea JE, Waugh DS, Byrd RA Biochemistry. 2007 Dec 11;46(49):13975-82. Epub 2007 Nov 15. PMID:18001134 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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