Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor

Nature ◽  
10.1038/23512 ◽  
1999 ◽  
Vol 400 (6746) ◽  
pp. 787-792 ◽  
Author(s):  
Kyeong Kyu Kim ◽  
Hisao Yokota ◽  
Sung-Hou Kim
Keyword(s):  
Cytoplasmic Domain ◽  
Helical Bundle ◽  
Four Helical Bundle ◽  
Bundle Structure

scholarly journals Backbone dynamics measurements on leukemia inhibitory factor, a rigid four-helical bundle cytokine

2008 ◽  
Vol 9 (4) ◽  
pp. 671-682 ◽  
Author(s):  
Shenggen Yao ◽  
David K. Smith ◽  
Mark G. Hinds ◽  
Jian-Guo Zhang ◽  
Nicos A. Nicola ◽  
...  
Keyword(s):  
Leukemia Inhibitory Factor ◽  
Inhibitory Factor ◽  
Backbone Dynamics ◽  
Helical Bundle ◽  
Four Helical Bundle

scholarly journals 1H-15N-NMR studies of bacteriorhodopsin Halobacterium halobium. Conformational dynamics of the four-helical bundle

1992 ◽  
Vol 210 (1) ◽  
pp. 223-229 ◽  
Author(s):  
Vladislav Yu. OREKHOV ◽  
Galina V. ABDULAEVA ◽  
Larisa Yu. MUSINA ◽  
Alexander S. ARSENIEV
Keyword(s):  
Conformational Dynamics ◽  
15N Nmr ◽  
Halobacterium Halobium ◽  
Nmr Studies ◽  
Helical Bundle ◽  
Four Helical Bundle

scholarly journals Crystal structures of MW1337R and lin2004: Representatives of a novel protein family that adopt a four-helical bundle fold

2008 ◽  
Vol 71 (3) ◽  
pp. 1589-1596 ◽  
Author(s):  
Piotr Kozbial ◽  
Qingping Xu ◽  
Hsiu-Ju Chiu ◽  
Daniel McMullan ◽  
S. Sri Krishna ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Protein Family ◽  
Helical Bundle ◽  
Four Helical Bundle ◽  
Novel Protein

scholarly journals First eight residues of apolipoprotein A-I mediate the C-terminus control of helical bundle unfolding and its lipidation

2019 ◽  
Author(s):  
Gregory Brubaker ◽  
Shuhui W. Lorkowski ◽  
Kailash Gulshan ◽  
Stanley L. Hazen ◽  
Valentin Gogonea ◽  
...  
Keyword(s):  
Cholesterol Efflux ◽  
Thermal Denaturation ◽  
Point Mutations ◽  
Lipid Binding ◽  
Site Directed Mutagenesis ◽  
Amino Terminus ◽  
Helical Bundle ◽  
Apolipoprotein A ◽  
C Terminus ◽  
Bundle Structure

AbstractThe crystal structure of a C-terminal deletion of apolipoprotein A-I (apoA1) shows a large helical bundle structure in the amino half of the protein, from residues 8 to 115. Using site directed mutagenesis, guanidine or thermal denaturation, cell free liposome clearance, and cellular ABCA1-mediated cholesterol efflux assays, we demonstrate that apoA1 lipidation can occur when the barrier to this bundle unfolding is lowered. The absence of the C-terminus renders the bundle harder to unfold resulting in loss of apoA1 lipidation that can be reversed by point mutations, such as Trp8Ala, and by truncations as short as 8 residues in the amino terminus, both of which lower the barrier to helical bundle unfolding. Locking the bundle via a disulfide bond leads to loss of apoA1 lipidation. We propose a model in which the C-terminus acts on the N-terminus to destabilize helical bundle. Upon lipid binding to the C-terminus, Trp8 is displaced from its interaction with Phe57, Arg61, Leu64, Val67, Phe71, and Trp72 to destabilize the bundle. However, when the C-terminus is deleted, Trp8 cannot be displaced, the bundle cannot unfold, and apoA1 cannot be lipidated.

scholarly journals Conservation of Helical Bundle Structure between the Exocyst Subunits

PLoS ONE ◽  
2009 ◽  
Vol 4 (2) ◽  
pp. e4443 ◽  
Author(s):  
Nicole J. Croteau ◽  
Melonnie L. M. Furgason ◽  
Damien Devos ◽  
Mary Munson
Keyword(s):  
Helical Bundle ◽  
Bundle Structure

Fast Folding of a Four-Helical Bundle Protein

2002 ◽  
Vol 124 (33) ◽  
pp. 9744-9750 ◽  
Author(s):  
Neelan J. Marianayagam ◽  
Farid Khan ◽  
Louise Male ◽  
Sophie E. Jackson
Keyword(s):  
Helical Bundle ◽  
Four Helical Bundle ◽  
Bundle Protein

Properties of transmembrane helix TM1 of the DcuS sensor kinase of Escherichia coli, the stator for TM2 piston signaling

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Marius Stopp ◽  
Philipp A. Steinmetz ◽  
Gottfried Unden
Keyword(s):  
Escherichia Coli ◽  
Transmembrane Helix ◽  
Structural Response ◽  
Sensor Kinase ◽  
Structural Adaptation ◽  
Helical Bundle ◽  
Structural And Functional Properties ◽  
Four Helical Bundle ◽  
Two Hybrid ◽  
Membrane Region

Abstract The sensor kinase DcuS of Escherichia coli perceives extracellular fumarate by a periplasmic PASP sensor domain. Transmembrane (TM) helix TM2, present as TM2-TM2′ homo-dimer, transmits fumarate activation in a piston-slide across the membrane. The second TM helix of DcuS, TM1, is known to lack piston movement. Structural and functional properties of TM1 were analyzed. Oxidative Cys-crosslinking (CL) revealed homo-dimerization of TM1 over the complete membrane, but only the central part showed α-helical +3/+4 spacing of the CL maxima. The GALLEX bacterial two-hybrid system indicates TM1/TM1′ interaction, and the presence of a TM1-TM1′ homo-dimer is suggested. The peripheral TM1 regions presented CL in a spacing atypical for α-helical arrangement. On the periplasmic side the deviation extended over 11 AA residues (V32-S42) between the α-helical part of TM1 and the onset of PASP. In the V32-S42 region, CL efficiency decreased in the presence of fumarate. Therefore, TM1 exists as a homo-dimer with α-helical arrangement in the central membrane region, and non-α-helical arrangement in the connector to PASP. The fumarate induced structural response in the V32-S42 region is suggested to represent a structural adaptation to the shift of TM2 in the TM1-TM1′/TM2-TM2′ four-helical bundle.

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