1WAZ

NMR Structure Determination of the bacterial mercury transporter, MerF, in micelles

1WAZ の概要

• エントリーDOI: 10.2210/pdb1waz/pdb
• 分子名称: MERF (1 entity in total)
• 機能のキーワード: protein structure, residual dipolar coupling, polytopic membrane protein, transport protein, antibiotic resistance, mercury detoxification
• 由来する生物種: MORGANELLA MORGANII
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4945.95

構造登録者

Howell, S.C.,Mesleh, M.F.,Opella, S.J. (登録日: 2004-10-28, 公開日: 2005-04-11, 最終更新日: 2024-05-15)

主引用文献

Howell, S.C.,Mesleh, M.F.,Opella, S.J.
NMR Structure Determination of a Membrane Protein with Two Transmembrane Helices in Micelles: Merf of the Bacterial Mercury Detoxification System
Biochemistry, 44:5196-, 2005

PubMed Abstract: 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.

PubMed: 15794657
DOI: 10.1021/BI048095V

実験手法

SOLUTION NMR