scholarly journals An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein

2015 ◽  
Vol 24 (6) ◽  
pp. 956-975 ◽  
Author(s):  
Michael C. Thompson ◽  
Duilio Cascio ◽  
David J. Leibly ◽  
Todd O. Yeates
Keyword(s):  
Substrate Binding ◽  
Shell Protein ◽  
Pore Opening ◽  
Allosteric Model

scholarly journals A Model for Allosteric Control of Pore Opening by Substrate Binding in the Eutl Microcompartment Shell Protein

2014 ◽  
Vol 106 (2) ◽  
pp. 652a-653a
Author(s):  
Michael C. Thompson ◽  
Sunny Chun ◽  
Todd O. Yeates
Keyword(s):  
Substrate Binding ◽  
Allosteric Control ◽  
Shell Protein ◽  
Pore Opening

scholarly journals Energy landscape steering in SecYEG mediates dynamic coupling in ATP driven protein translocation

2019 ◽  
Author(s):  
Joel A. Crossley ◽  
Tomas Fessl ◽  
Matthew A. Watson ◽  
Daniel W. Watkins ◽  
Robin A. Corey ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Conformational Changes ◽  
Protein Translocation ◽  
Energy Landscape ◽  
Membrane Pore ◽  
Reaction Coordinates ◽  
Allosteric Communication ◽  
Pore Opening ◽  
Lateral Gate ◽  
Allosteric Model

AbstractThe Sec translocon is a transmembrane assembly highly conserved among all forms of life as the principal route for transport of polypeptides across or into lipid bilayers. In bacteria translocation involves allosteric communication between the membrane pore SecYEG and the associated SecA ATPase. Using singlemolecule fluorescence we reveal that slow conformational changes associated with the ATPase SecA modulate fast opening and closure of the SecY lateral gate. Such a mismatch of timescales is not compatible with direct coupling between SecA and SecYEG. A dynamic allosteric model is proposed in which the SecA ATPase cycle ‘steers’ the energy landscape for SecY pore opening. We map the experimental traces onto reduced reaction coordinates derived from molecular dynamics trajectories, providing a model for the energy landscape and a structural interpretation of the associated dynamics. Dynamic allostery may be common among motor ATPases that drive conformational changes in molecular machines.Graphical TOC Entry

Fibronexus-Like Adhesion Sites are Present at the Invasive Zones of Human Epidermoid Carcinomas

1982 ◽  
Vol 40 ◽  
pp. 106-109
Author(s):  
Irwin I. Singer
Keyword(s):  
Cell Cycle ◽  
Serum Concentration ◽  
Substrate Binding ◽  
High Serum ◽  
Adhesion Sites ◽  
Substrate Adhesion ◽  
Focal Contacts ◽  
Adhesion Complex ◽  
Low Serum

Our previous results indicate that two types of fibronectin-cytoskeletal associations may be formed at the fibroblast surface: dorsal matrixbinding fibronexuses generated in high serum (5% FBS) cultures, and ventral substrate-adhering units formed in low serum (0.3% FBS) cultures. The substrate-adhering fibronexus consists of at least vinculin (VN) and actin in its cytoplasmic leg, and fibronectin (FN) as one of its major extracellular components. This substrate-adhesion complex is localized in focal contacts, the sites of closest substratum approach visualized with interference reflection microscopy, which appear to be the major points of cell-tosubstrate adhesion. In fibroblasts, the latter substrate-binding complex is characteristic of cultures that are arrested at the G1 phase of the cell cycle due to the low serum concentration in their medium. These arrested fibroblasts are very well spread, flattened, and immobile.

Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase

2001 ◽  
Vol 268 (6) ◽  
pp. 1640-1645
Author(s):  
Annelise Matharu ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
Bruno Maras ◽  
Robert A. John
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Aminotransferase ◽  
Substrate Binding ◽  
Arginine Residues

Hydrogen Sulfide Inhibits Calcium-Induced Mitohondrial Permeability Transition Pore Opening in the Heart of Adult and Old Rats

2012 ◽  
Vol 3 (2) ◽  
pp. 135-147 ◽  
Author(s):  
Nataliya A. Strutynska ◽  
Olena M. Semenykhina ◽  
Snizhana V. Chorna ◽  
Galyna L. Vavilova ◽  
Vadim F. Sagach
Keyword(s):  
Hydrogen Sulfide ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Permeability Transition Pore Opening ◽  
Pore Opening ◽  
Old Rats

Copper–oxygen Dynamics in Tyrosinase

2019 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Sachiko Yanagisawa ◽  
Minoru Kubo ◽  
Genji Kurisu ◽  
Shinobu Itoh
Keyword(s):  
Catalytic Mechanism ◽  
Substrate Binding ◽  
Active Form ◽  
Copper Ion ◽  
Atomic Resolution ◽  
Oxygen Species ◽  
X Ray ◽  
Oxygen Dynamics ◽  
Insight Into ◽  
Copper Centre

To unveil the activation of dioxygen on the copper centre (Cu<sub>2</sub>O<sub>2</sub>core) of tyrosinase, we performed X-ray crystallograpy with active-form tyrosinase at near atomic resolution. This study provided a novel insight into the catalytic mechanism of the tyrosinase, including the rearrangement of copper-oxygen species as well as the intramolecular migration of copper ion induced by substrate-binding.<br>

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