1waz
From Proteopedia
|
NMR STRUCTURE DETERMINATION OF THE BACTERIAL MERCURY TRANSPORTER, MERF, IN MICELLES
Overview
The three-dimensional backbone structure of a membrane protein with two transmembrane helices in micelles was determined using solution NMR methods that rely on the measurement of backbone (1)H-(15)N residual dipolar couplings (RDCs) from samples of two different constructs that align differently in stressed polyacrylamide gels. Dipolar wave fitting to the (1)H-(15)N RDCs determines the helical boundaries based on periodicity and was utilized in the generation of supplemental dihedral restraints for the helical segments. The (1)H-(15)N RDCs and supplemental dihedral restraints enable the determination of the structure of the helix-loop-helix core domain of the mercury transport membrane protein MerF with a backbone RMSD of 0.58 A. Moreover, the fold of this polypeptide demonstrates that the two vicinal pairs of cysteine residues, shown to be involved in the transport of Hg(II) across the membrane, are exposed to the cytoplasm. This finding differs from earlier structural and mechanistic models that were based primarily on the somewhat atypical hydropathy plot for MerF and related transport proteins.
About this Structure
1WAZ is a Single protein structure of sequence from Morganella morganii. Full crystallographic information is available from OCA.
Reference
NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system., Howell SC, Mesleh MF, Opella SJ, Biochemistry. 2005 Apr 5;44(13):5196-206. PMID:15794657
Page seeded by OCA on Thu Feb 21 15:42:24 2008
