2jvp
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(New page: 200px<br /><applet load="2jvp" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jvp" /> '''Complete Chemical Shift Assignments and XPLO...)
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Revision as of 09:58, 23 January 2008
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Complete Chemical Shift Assignments and XPLOR restraints for YmoA
Overview
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.
About this Structure
2JVP is a Single protein structure of sequence from Yersinia pestis. Full crystallographic information is available from OCA.
Reference
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 Nov 15;. PMID:18001134
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