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2MOZ

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

Summary for 2MOZ
Entry DOI10.2210/pdb2moz/pdb
Related2M67
NMR InformationBMRB: 19115
DescriptorMerF (1 entity in total)
Functional Keywordsmembrane protein, membrane protein structures by solution nmr, mpsbynmr, psi-biology, structural genomics
Biological sourceMorganella morganii
Total number of polymer chains1
Total formula weight8670.40
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 citationTian, 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: 25103921
DOI: 10.1007/s10858-014-9852-0
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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