2MOZ
Structure of the Membrane Protein MerF, a Bacterial Mercury Transporter, Improved by the Inclusion of Chemical Shift Anisotropy Constraints
Summary for 2MOZ
| Entry DOI | 10.2210/pdb2moz/pdb |
| Related | 2M67 |
| NMR Information | BMRB: 19115 |
| Descriptor | MerF (1 entity in total) |
| Functional Keywords | membrane protein, membrane protein structures by solution nmr, mpsbynmr, psi-biology, structural genomics |
| Biological source | Morganella morganii |
| Total number of polymer chains | 1 |
| Total formula weight | 8670.40 |
| Authors | Tian, Y.,Lu, G.J.,Marassi, F.M.,Opella, S.J.,Membrane Protein Structures by Solution NMR (MPSbyNMR) (deposition date: 2014-05-07, release date: 2014-07-30, Last modification date: 2024-05-15) |
| Primary citation | Tian, Y.,Lu, G.J.,Marassi, F.M.,Opella, S.J. Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints. J.Biomol.Nmr, 60:67-71, 2014 Cited by PubMed Abstract: 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. PubMed: 25103921DOI: 10.1007/s10858-014-9852-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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