Rebinding of the extrinsic proteins of Photosystem II studied by electron microscopy and single particle alignment: an assessment with small two-dimensional ordered arrays of Photosystem II

Rosenberg, Mark F.; Holzenburg, Andreas; Shepherd, Fiona H.; Nicholson, William V.; Flint, Toby D.; Ford, Robert C.

doi:10.1016/s0005-2728(96)00124-7

Cited by 6 publications

(3 citation statements)

References 49 publications

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“…The asterisks show two densities related by 2-fold pseudosymmetry. The third NH 2 -terminal MSD of MRP1 might be expected to reduce any pseudo-2-fold symmetry (40). An indication from these projection maps for such behavior is in Fig.…”

Section: Resultsmentioning

confidence: 90%

The Structure of the Multidrug Resistance Protein 1 (MRP1/ABCC1)

Rosenberg

Mao

Holzenburg

et al. 2001

Journal of Biological Chemistry

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149

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Multidrug resistance protein 1 (MRP1/ABCC1) is an ATP-binding cassette (ABC) polytopic membrane transporter of considerable clinical importance that confers multidrug resistance on tumor cells by reducing drug accumulation by active efflux. MRP1 is also an efficient transporter of conjugated organic anions. Like other ABC proteins, including the drug resistance conferring 170-kDa P-glycoprotein (ABCB1), the 190-kDa MRP1 has a core structure consisting of two membrane-spanning domains (MSDs), each followed by a nucleotide binding domain (NBD). However, unlike P-glycoprotein and most other ABC superfamily members, MRP1 contains a third MSD with five predicted transmembrane segments with an extracytosolic NH 2 terminus. Moreover, the two nucleotide-binding domains of MRP1 are considerably more divergent than those of P-glycoprotein. In the present study, the first structural details of MRP1 purified from drug-resistant lung cancer cells have been obtained by electron microscopy of negatively stained single particles and two-dimensional crystals formed after reconstitution of purified protein with lipids. The crystals display p2 symmetry with a single dimer of MRP1 in the unit cell. The overall dimensions of the MRP1 monomer are ϳ80 ؋ 100 Å. The MRP1 monomer shows some pseudo-2-fold symmetry in projection, and in some orientations of the detergent-solubilized particles, displays a stain filled depression (putative pore) appearing toward the center of the molecule, presumably to enable transport of substrates. These data represent the first structural information of this transporter to ϳ22-Å resolution and provide direct structural evidence for a dimeric association of the transporter in a reconstituted lipid bilayer.The 190-kDa multidrug resistance protein MRP1 1 (ABCC1) is a polytopic membrane transport protein that belongs to the ATP-binding cassette (ABC) superfamily and has been detected in many different drug-resistant cell lines and tumor tissues since it was first cloned in 1992 (1-6). When overexpressed in tumor cells, MRP1 confers multidrug resistance by reducing intracellular drug concentrations in an ATP-dependent manner (6 -8). In this respect, MRP1 is similar to another ABC transporter, the well characterized 170-kDa P-glycoprotein (Pgp) (ABCB1) (9, 10). ABC proteins play important physiological and protective functions in bacteria, yeast, plants, and mammals and are capable of transporting a wide variety of molecules across biological membranes. Known substrates for ABC transporters include ions, phospholipids, steroids, polysaccharides, amino acids, peptides, and in the case of several MRPrelated proteins, anionic conjugated endo-and xenobiotics (6, 10 -12). In addition to MRP1 and P-gp, other examples of clinically important human ABC proteins include the cystic fibrosis transmembrane conductance regulator CFTR (13), and the sulfonylurea receptor (SUR), which is part of an ATPsensitive potassium channel involved in insulin secretion (14).The amino acid sequence of MRP1 predicts that it contains a cor...

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Section: Resultsmentioning

confidence: 90%

The Structure of the Multidrug Resistance Protein 1 (MRP1/ABCC1)

Rosenberg

Mao

Holzenburg

et al. 2001

Journal of Biological Chemistry

Self Cite

149

111

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“…This fits the structural and biochemical data, where PSII core complexes can be observed in one discrete plane and membrane fraction, and LHCII complexes can be observed in another membrane fraction. A survey of previous structural studies of thylakoid membranes [13,16,17,21, 29–32] suggests that they may be newly interpreted in terms of the alternative model of thylakoid structure. A review of these studies is beyond the scope of this paper and will be presented elsewhere.…”

Section: Discussionmentioning

confidence: 99%

An alternative model for photosystem II/light harvesting complex II in grana membranes based on cryo‐electron microscopy studies

Ford

Stoylova

Holzenburg

2002

European Journal of Biochemistry

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The photosynthetic protein complexes in plants are located in the chloroplast thylakoid membranes. These membranes have an ultrastructure that consists of tightly stacked ÔgranaÕ regions interconnected by unstacked membrane regions. The structure of isolated grana membranes has been studied here by cryo-electron microscopy. The data reveals an unusual arrangement of the photosynthetic protein complexes, staggered over two tightly stacked planes. Chaotrope treatment of the paired grana membranes has allowed the separation and isolation of two biochemically distinct membrane fractions. These data have led us to an alternative model of the ultrastructure of the grana where segregation exists within the grana itself. This arrangement would change the existing view of plant photosynthesis, and suggests potential links between cyanobacterial and plant photosystem II light harvesting systems.

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“…Images were contrast normalized, band pass filtered, and aligned by reference-free alignment (18). Classes of particles representing identical orientations were determined by multivariate statistical analysis and hierarchical ascendant classification with complete linkage (5,20,28). Resolution was assessed by using the Fourier ring correlation criterion (26).…”

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confidence: 99%

Three-Dimensional Structure of Herpes Simplex Virus Type 1 Glycoprotein D at 2.4-Nanometer Resolution

Pilling

Rosenberg

Willis³

et al. 1999

J Virol

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Herpes simplex virus type 1 glycoprotein D (gD) is essential for virus infectivity and is responsible for binding to cellular membrane proteins and subsequently promoting fusion between the virus envelope and the cell. No structural data are available for gD or for any other herpesvirus envelope protein. Here we present a three-dimensional model for the baculovirus-expressed truncated protein gD1(306t) based on electron microscopic data. We demonstrate that gD1(306t) appears as a homotetramer containing a pronounced pocket in the center of the molecule. Monoclonal antibody binding demonstrates that the molecule is oriented such that the pocket protrudes away from the virus envelope.

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Rebinding of the extrinsic proteins of Photosystem II studied by electron microscopy and single particle alignment: an assessment with small two-dimensional ordered arrays of Photosystem II

Cited by 6 publications

References 49 publications

The Structure of the Multidrug Resistance Protein 1 (MRP1/ABCC1)

The Structure of the Multidrug Resistance Protein 1 (MRP1/ABCC1)

An alternative model for photosystem II/light harvesting complex II in grana membranes based on cryo‐electron microscopy studies

Three-Dimensional Structure of Herpes Simplex Virus Type 1 Glycoprotein D at 2.4-Nanometer Resolution

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