2moz | pdb_00002moz

Structure of the Membrane Protein MerF, a Bacterial Mercury Transporter, Improved by the Inclusion of Chemical Shift Anisotropy Constraints

spinqualitylabelsall models 2moz Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2moz is a 1 chain structure with sequence from Morganella morganii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q56446_MORMO Publication Abstract from PubMed MerF is a mercury transport membrane protein from the bacterial mercury detoxification system. By performing a solid-state INEPT experiment and measuring chemical shift anisotropy frequencies in aligned samples, we are able to improve on the accuracy and precision of the initial structure that we presented. MerF has four N-terminal and eleven C-terminal residues that are mobile and unstructured in phospholipid bilayers. The structure presented here has average pairwise RMSDs of 1.78 A for heavy atoms and 0.92 A for backbone atoms. Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints.,Tian Y, Lu GJ, Marassi FM, Opella SJ J Biomol NMR. 2014 Sep;60(1):67-71. doi: 10.1007/s10858-014-9852-0. Epub 2014 Aug , 8. PMID:25103921 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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