ArticleProtein science : a publication of the Protein Society2009
Backbone structure of a small helical integral membrane protein: A unique structural characterization.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 41 citations in OpenAlex.
- The Transmembrane Conformation of the Influenza B Virus M2 Protein in Lipid Bilayers.Scientific reports · 2019Article
- Structural characterization of a protein adsorbed on aluminum hydroxide adjuvant in vaccine formulation.NPJ vaccines · 2019Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Preserved Transmembrane Segment Topology, Structure, and Dynamics in Disparate Micellar Environments.The journal of physical chemistry letters · 2017Article
- The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Journal of molecular biology · 2016Article
- Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA).Journal of biomolecular NMR · 2015Article
- Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Advances in NMR structures of integral membrane proteins.Current opinion in structural biology · 2013Review
- Solution NMR studies on the orientation of membrane-bound peptides and proteins by paramagnetic probes.Molecules (Basel, Switzerland) · 2013Review
- Facile backbone structure determination of human membrane proteins by NMR spectroscopy.Nature methods · 2012Article
- Expression and purification of the p75 neurotrophin receptor transmembrane domain using a ketosteroid isomerase tag.Microbial cell factories · 2012Article
- Identification and removal of nitroxide spin label contaminant: impact on PRE studies of α-helical membrane proteins in detergent.Protein science : a publication of the Protein Society · 2012Article
- Rapid exploration of the folding topology of helical membrane proteins using paramagnetic perturbation.Protein science : a publication of the Protein Society · 2010Article
- Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
- Charged or aromatic anchor residue dependence of transmembrane peptide tilt.The Journal of biological chemistry · 2010Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The structural characterization of small integral membrane proteins pose a significant challenge for structural biology because of the multitude of molecular interactions between the protein and its heterogeneous environment. Here, the three-dimensional backbone structure of Rv1761c from Mycobacterium tuberculosis has been characterized using solution NMR spectroscopy and dodecylphosphocholine (DPC) micelles as a membrane mimetic environment. This 127 residue single transmembrane helix protein has a significant (10 kDa) C-terminal extramembranous domain. Five hundred and ninety distance, backbone dihedral, and orientational restraints were employed resulting in a 1.16 A rmsd backbone structure with a transmembrane domain defined at 0.40 A. The structure determination approach utilized residual dipolar coupling orientation data from partially aligned samples, long-range paramagnetic relaxation enhancement derived distances, and dihedral restraints from chemical shift indices to determine the global fold. This structural model of Rv1761c displays some influences by the membrane mimetic illustrating that the structure of these membrane proteins is dictated by a combination of the amino acid sequence and the protein's environment. These results demonstrate both the efficacy of the structural approach and the necessity to consider the biophysical properties of membrane mimetics when interpreting structural data of integral membrane proteins and, in particular, small integral membrane proteins.
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