Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints. J Biomol NMR 2014 Sep;60(1):67-71
Date
08/12/2014Pubmed ID
25103921Pubmed Central ID
PMC4154067DOI
10.1007/s10858-014-9852-0Scopus ID
2-s2.0-84929129611 (requires institutional sign-in at Scopus site) 17 CitationsAbstract
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 Å for heavy atoms and 0.92 Å for backbone atoms.
Author List
Tian Y, Lu GJ, Marassi FM, Opella SJAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnisotropyBacterial Proteins
Cation Transport Proteins
Escherichia coli
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Recombinant Proteins
