Structural Characterization of the Transmembrane Domain from Subunit e of Yeast F1Fo-ATP Synthase:  A Helical GXXXG Motif Located Just under the Micelle Surface†

Biochemistry ◽  
2008 ◽  
Vol 47 (7) ◽  
pp. 1910-1917 ◽  
Author(s):  
Huili Yao ◽  
Rosemary A. Stuart ◽  
Sheng Cai ◽  
Daniel S. Sem
Keyword(s):  
Atp Synthase ◽  
Structural Characterization ◽  
Transmembrane Domain ◽  
F1fo Atp Synthase ◽  
Gxxxg Motif ◽  
Subunit E ◽  
Micelle Surface

The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane

2003 ◽  
Vol 270 (8) ◽  
pp. 1875-1884 ◽  
Author(s):  
Genevieve Arselin ◽  
Marie-France Giraud ◽  
Alain Dautant ◽  
Jacques Vaillier ◽  
Daniel Brethes ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Mitochondrial Membrane ◽  
Transmembrane Domain ◽  
Gxxxg Motif ◽  
Subunit E

scholarly journals The Stator Complex of the A1A0-ATP Synthase—Structural Characterization of the E and H Subunits

2008 ◽  
Vol 375 (3) ◽  
pp. 673-685 ◽  
Author(s):  
Erik Kish-Trier ◽  
Lee-Ann K. Briere ◽  
Stanley D. Dunn ◽  
Stephan Wilkens
Keyword(s):  
Atp Synthase ◽  
Structural Characterization

Structural Characterization of the Interaction of the δ and α Subunits of theEscherichia coliF1F0-ATP Synthase by NMR Spectroscopy†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (35) ◽  
pp. 11786-11794 ◽  
Author(s):  
Stephan Wilkens ◽  
Dan Borchardt ◽  
Joachim Weber ◽  
Alan E. Senior
Keyword(s):  
Nmr Spectroscopy ◽  
Atp Synthase ◽  
Structural Characterization ◽  
Α Subunits

scholarly journals Structural characterization of triple transmembrane domain containing fragments of a yeast G protein-coupled receptor in an organic : aqueous environment by solution-state NMR spectroscopy

2015 ◽  
Vol 21 (3) ◽  
pp. 212-222 ◽  
Author(s):  
Katrina E. Fracchiolla ◽  
Leah S. Cohen ◽  
Boris Arshava ◽  
Martin Poms ◽  
Oliver Zerbe ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
G Protein ◽  
Structural Characterization ◽  
Transmembrane Domain ◽  
Aqueous Environment ◽  
G Protein Coupled Receptor ◽  
Solution State ◽  
G Protein Coupled

scholarly journals Structural Characterization of the Amyloid Precursor Protein Transmembrane Domain and Its γ-Cleavage Site

ACS Omega ◽  
2017 ◽  
Vol 2 (10) ◽  
pp. 6525-6534 ◽  
Author(s):  
Anna Itkin ◽  
Evgeniy S. Salnikov ◽  
Christopher Aisenbrey ◽  
Jesus Raya ◽  
Elise Glattard ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Structural Characterization ◽  
Cleavage Site ◽  
Transmembrane Domain ◽  
Precursor Protein

scholarly journals Structural characterization of the mycobacterial ATP synthase c-ring and its interaction with the novel anti-tuberculosis drug bedaquiline

2016 ◽  
Vol 72 (a1) ◽  
pp. s210-s210
Author(s):  
Laura Preiss ◽  
Bianca Eisel ◽  
Ernst Grell ◽  
Luise Eckhardt-Strelau ◽  
Özkan Yildiz ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Structural Characterization ◽  
The Novel

Structural characterization of CD81–Claudin-1 hepatitis C virus receptor complexes

2011 ◽  
Vol 39 (2) ◽  
pp. 537-540 ◽  
Author(s):  
Nicklas Bonander ◽  
Mohammed Jamshad ◽  
Ke Hu ◽  
Michelle J. Farquhar ◽  
Zania Stamataki ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Structural Characterization ◽  
Biological Function ◽  
Transmembrane Domain ◽  
Therapeutic Agents ◽  
Lateral Movement ◽  
Receptor Complexes ◽  
Major Structural Component

Tetraspanins are thought to exert their biological function(s) by co-ordinating the lateral movement and trafficking of associated molecules into tetraspanin-enriched microdomains. A second four-TM (transmembrane) domain protein family, the Claudin superfamily, is the major structural component of cellular TJs (tight junctions). Although the Claudin family displays low sequence homology and appears to be evolutionarily distinct from the tetraspanins, CD81 and Claudin-1 are critical molecules defining HCV (hepatitis C virus) entry; we recently demonstrated that CD81–Claudin-1 complexes have an essential role in this process. To understand the molecular basis of CD81–Claudin-1 complex formation, we produced and purified milligram quantities of full-length CD81 and Claudin-1, alone and in complex, in both detergent and lipid contexts. Structural characterization of these purified proteins will allow us to define the mechanism(s) underlying virus–cell interactions and aid the design of therapeutic agents targeting early steps in the viral life cycle.

The transmembrane domain of subunit b of the Escherichia coli F1FO ATP synthase is sufficient for H+-translocating activity together with subunits a and c

2004 ◽  
Vol 271 (14) ◽  
pp. 3036-3042 ◽  
Author(s):  
Jörg-Christian Greie ◽  
Thomas Heitkamp ◽  
Karlheinz Altendorf
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Transmembrane Domain ◽  
F1fo Atp Synthase ◽  
Subunit B
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