Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tian Y, Lu GJ, Marassi FM, Opella SJ. 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. PMID:25103921 doi:10.1007/s10858-014-9852-0
