scholarly journals Crystal Structure of SecDF, a Sec Translocon-associated Membrane Protein

2011 ◽  
Vol 51 (5) ◽  
pp. 236-237
Author(s):  
Tomoya TSUKAZAKI
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Sec Translocon

scholarly journals Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex

1998 ◽  
Vol 95 (20) ◽  
pp. 11673-11678 ◽  
Author(s):  
L.- O. Essen ◽  
R. Siegert ◽  
W. D. Lehmann ◽  
D. Oesterhelt
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Lipid Complex

scholarly journals Crystal Structure of the Outer Membrane Protein OpdK from Pseudomonas aeruginosa

Structure ◽  
2008 ◽  
Vol 16 (7) ◽  
pp. 1027-1035 ◽  
Author(s):  
Shyamasri Biswas ◽  
Mohammad M. Mohammad ◽  
Liviu Movileanu ◽  
Bert van den Berg
Keyword(s):  
Crystal Structure ◽  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein

scholarly journals In vitro membrane protein synthesis inside Sec translocon-reconstituted cell-sized liposomes

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Naoki Ohta ◽  
Yasuhiko Kato ◽  
Hajime Watanabe ◽  
Hirotada Mori ◽  
Tomoaki Matsuura
Keyword(s):  
Protein Synthesis ◽  
Membrane Protein ◽  
Sec Translocon

scholarly journals Evaluation of a Structural Model ofPseudomonas aeruginosa Outer Membrane Protein OprM, an Efflux Component Involved in Intrinsic Antibiotic Resistance

2001 ◽  
Vol 183 (1) ◽  
pp. 367-374 ◽  
Author(s):  
Kendy K. Y. Wong ◽  
Fiona S. L. Brinkman ◽  
Roland S. Benz ◽  
Robert E. W. Hancock
Keyword(s):  
Crystal Structure ◽  
Antibiotic Resistance ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Structural Model ◽  
Sequence Similarity ◽  
Homologous Protein ◽  
Related Family ◽  
Resistance Nodulation Division

ABSTRACT The outer membrane protein OprM of Pseudomonas aeruginosa is involved in intrinsic and mutational multiple-antibiotic resistance as part of two resistance-nodulation-division efflux systems. The crystal structure of TolC, a homologous protein in Escherichia coli, was recently published (V. Koronakis, A. Sharff, E. Koronakis, B. Luisl, and C. Hughes, Nature 405:914–919, 2000), demonstrating a distinctive architecture comprising outer membrane β-barrel and periplasmic helical-barrel structures, which assemble differently from the common β-barrel-only conformation of porins. Based on their sequence similarity, a similar content of α-helical and β-sheet structure determined by circular dichroism spectroscopy, and our observation that OprM, like TolC, reconstitutes channels in planar bilayer membranes, OprM and TolC were considered to be structurally homologous, and a model of OprM was constructed by threading its sequence to the TolC crystal structure. Residues thought to be important for the TolC structure were conserved in space in this OprM model. Analyses of deletion mutants and previously isolated insertion mutants of OprM in the context of this model allowed us to propose roles for different protein domains. Our data indicate that the helical barrel of the protein is critical for both the function and the integrity of the protein, while a C-terminal domain localized around the equatorial plane of this helical barrel is dispensable. Extracellular loops appear to play a lesser role in substrate specificity for this efflux protein compared to classical porins, and there appears to be a correlation between the change in antimicrobial activity for OprM mutants and the pore size. Our model and channel formation studies support the “iris” mechanism of action for TolC and permit us now to form more focused hypotheses about the functional domains of OprM and its related family of efflux proteins.

scholarly journals Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Kaoru Kumazaki ◽  
Toshiki Kishimoto ◽  
Arata Furukawa ◽  
Hiroyuki Mori ◽  
Yoshiki Tanaka ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Membrane Protein ◽  
Protein Chaperone
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