scholarly journals Three-dimensional structure of the human breast cancer resistance protein (BCRP/ABCG2) in an inward-facing conformation

2015 ◽  
Vol 71 (8) ◽  
pp. 1725-1735 ◽  
Author(s):  
Mark F. Rosenberg ◽  
Zsolt Bikadi ◽  
Eszter Hazai ◽  
Tobias Starborg ◽  
Lawrence Kelley ◽  
...  
Keyword(s):  
Drug Disposition ◽  
Three Dimensional ◽  
Structural Data ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
Cancer Resistance ◽  
Three Dimensional Structure ◽  
Binding Domains ◽  
Subtomogram Averaging ◽  
And Function

ABCG2 is an efflux drug transporter that plays an important role in drug resistance and drug disposition. In this study, the first three-dimensional structure of human full-length ABCG2 analysed by electron crystallography from two-dimensional crystals in the absence of nucleotides and transported substrates is reported at 2 nm resolution. In this state, ABCG2 forms a symmetric homodimer with a noncrystallographic twofold axis perpendicular to the two-dimensional crystal plane, as confirmed by subtomogram averaging. This configuration suggests an inward-facing configuration similar to murine ABCB1, with the nucleotide-binding domains (NBDs) widely separated from each other. In the three-dimensional map, densities representing the long cytoplasmic extensions from the transmembrane domains that connect the NBDs are clearly visible. The structural data have allowed the atomic model of ABCG2 to be refined, in which the two arms of the V-shaped ABCG2 homodimeric complex are in a more closed and narrower conformation. The structural data and the refined model of ABCG2 are compatible with the biochemical analysis of the previously published mutagenesis studies, providing novel insight into the structure and function of the transporter.

Three-Dimensional Structure of Cloned T3 Connector Protein at 1.6nm Resolution

1990 ◽  
Vol 48 (1) ◽  
pp. 282-283
Author(s):  
José L. Carrascosa ◽  
José M. Valpuesta ◽  
Hisao Fujisawa
Keyword(s):  
Dna Sequences ◽  
Expression Vector ◽  
Three Dimensional ◽  
Deae Cellulose ◽  
Dna Packaging ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
Freezing And Thawing ◽  
Three Dimensional Structure ◽  
Dimensional Reconstruction

The head to tail connector of bacteriophages plays a fundamental role in the assembly of viral heads and DNA packaging. In spite of the absence of sequence homology, the structure of connectors from different viruses (T4, Ø29, T3, P22, etc) share common morphological features, that are most clearly revealed in their three-dimensional structure. We have studied the three-dimensional reconstruction of the connector protein from phage T3 (gp 8) from tilted view of two dimensional crystals obtained from this protein after cloning and purification.DNA sequences including gene 8 from phage T3 were cloned, into Bam Hl-Eco Rl sites down stream of lambda promotor PL, in the expression vector pNT45 under the control of cI857. E R204 (pNT89) cells were incubated at 42°C for 2h, harvested and resuspended in 20 mM Tris HC1 (pH 7.4), 7mM 2 mercaptoethanol, ImM EDTA. The cells were lysed by freezing and thawing in the presence of lysozyme (lmg/ml) and ligthly sonicated. The low speed supernatant was precipitated by ammonium sulfate (60% saturated) and dissolved in the original buffer to be subjected to gel nitration through Sepharose 6B, followed by phosphocellulose colum (Pll) and DEAE cellulose colum (DE52). Purified gp8 appeared at 0.3M NaCl and formed crystals when its concentration increased above 1.5 mg/ml.

scholarly journals Impact of genetic variation on three dimensional structure and function of proteins

PLoS ONE ◽  
2017 ◽  
Vol 12 (3) ◽  
pp. e0171355 ◽  
Author(s):  
Roshni Bhattacharya ◽  
Peter W. Rose ◽  
Stephen K. Burley ◽  
Andreas Prlić
Keyword(s):  
Genetic Variation ◽  
Three Dimensional ◽  
Structure And Function ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
And Function

Assembled structures of tetrakis(biimidazole)dirhodium complexes hydrogen-bonded with common inorganic anions

2014 ◽  
Vol 70 (6) ◽  
pp. 1006-1019 ◽  
Author(s):  
Jin-Long ◽  
Kazuhiro Uemura ◽  
Masahiro Ebihara
Keyword(s):  
Hydrogen Bonding ◽  
Three Dimensional ◽  
Inorganic Anions ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
Discrete Structure ◽  
Torsion Angles ◽  
One Dimensional ◽  
Three Dimensional Structure ◽  
Dirhodium Complexes

Eight new structures of dirhodium complexes, each with four biimidazole (H2bim) ligands, were obtained: [Rh2(H2bim)4(H2O)2](NO3)4·4H2O (I), [Rh2(H2bim)4(H2O)2](ClO4)4·5H2O (II), [Rh2(H2bim)4(MeOH)2](ClO4)4(III), [Rh2(H2bim)4(DMF)2](BF4)4(IV), [Rh2(H2bim)4(Mepy)2](SiF6)2·8H2O (V), [{Rh2(H2bim)4(pz)}2(μ-pz)](SiF6)(ClO4)6·12.7H2O (VI), [{Rh2(H2bim)4(pz)}2(μ-pz)](ClO4)8·11.4H2O (VII) and [Rh2(H2bim)4(μ-pz)](SiF6)2·6H2O (VIII). The unbridged Rh—Rh bond distances range between 2.6313 (8) and 2.7052 (5) Å. The dirhodium units adopt a staggered conformation with torsion angles N—Rh—Rh—N of 37.6 (4)–48.98 (8)°. Various assembled structures were constructed by hydrogen bonding between the complexes and the anions: a discrete structure in (IV), one-dimensional structure in (II), two-dimensional structures in (I), (III), (VI), (VII) and (VIII) and a three-dimensional structure in (V).

scholarly journals Two-Dimensional Crystallization on Lipid Monolayers and Three-Dimensional Structure of Sticholysin II, a Cytolysin from the Sea Anemone Stichodactyla helianthus

2000 ◽  
Vol 78 (6) ◽  
pp. 3186-3194 ◽  
Author(s):  
Jaime Martín-Benito ◽  
Francisco Gavilanes ◽  
Vivian de los Ríos ◽  
José M. Mancheño ◽  
José J. Fernández ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Sea Anemone ◽  
Dimensional Structure ◽  
Lipid Monolayers ◽  
Two Dimensional ◽  
Three Dimensional Structure
Sign in / Sign up

Export Citation Format

Share Document