2mme: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q6XVY0_SHIFL Q6XVY0_SHIFL] | [https://www.uniprot.org/uniprot/Q6XVY0_SHIFL Q6XVY0_SHIFL] | ||
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== Publication Abstract from PubMed == | |||
We introduce a general hybrid approach for determining the structures of supramolecular assemblies. Cryo-electron microscopy (cryo-EM) data define the overall envelope of the assembly and rigid-body orientation of the subunits while solid-state nuclear magnetic resonance (ssNMR) chemical shifts and distance constraints define the local secondary structure, protein fold and inter-subunit interactions. Finally, Rosetta structure calculations provide a general framework to integrate the different sources of structural information. Combining a 7.7-A cryo-EM density map and 996 ssNMR distance constraints, the structure of the type-III secretion system needle of Shigella flexneri is determined to a precision of 0.4 A. The calculated structures are cross-validated using an independent data set of 691 ssNMR constraints and scanning transmission electron microscopy measurements. The hybrid model resolves the conformation of the non-conserved N terminus, which occupies a protrusion in the cryo-EM density, and reveals conserved pore residues forming a continuous pattern of electrostatic interactions, thereby suggesting a mechanism for effector protein translocation. | |||
High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.,Demers JP, Habenstein B, Loquet A, Kumar Vasa S, Giller K, Becker S, Baker D, Lange A, Sgourakis NG Nat Commun. 2014 Sep 29;5:4976. doi: 10.1038/ncomms5976. PMID:25264107<ref>PMID:25264107</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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