substrate docking
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2020 ◽  
Vol 253 (6) ◽  
pp. 563-576
Author(s):  
Ana-Nicoleta Bondar

AbstractTransmembrane substrate cleavage by the small Escherichia coli rhomboid protease GlpG informs on mechanisms by which lipid interactions shape reaction coordinates of membrane-embedded enzymes. Here, I review and discuss new work on the molecular picture of protein–lipid interactions that might govern the formation of the substrate–enzyme complex in fluid lipid membranes. Negatively charged PG-type lipids are of particular interest, because they are a major component of bacterial membranes. Atomistic computer simulations indicate POPG and DOPG lipids bridge remote parts of GlpG and might pre-occupy the substrate-docking site. Inhibition of catalytic activity by PG lipids could arise from ligand-like lipid binding at the active site, which could delay or prevent substrate docking. Dynamic protein–lipid H-bond networks, water access to the active site, and fluctuations in the orientation of GlpG suggest that GlpG has lipid-coupled dynamics that could shape the energy landscape of transmembrane substrate docking. Graphic Abstract



2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Laura E. Rosen ◽  
Joseph E. Klebba ◽  
Jonathan B. Asfaha ◽  
Chloe M. Ghent ◽  
Melody G. Campbell ◽  
...  

AbstractChromosome segregation begins when the cysteine protease, separase, cleaves the Scc1 subunit of cohesin at the metaphase-to-anaphase transition. Separase is inhibited prior to metaphase by the tightly bound securin protein, which contains a pseudosubstrate motif that blocks the separase active site. To investigate separase substrate specificity and regulation, here we develop a system for producing recombinant, securin-free human separase. Using this enzyme, we identify an LPE motif on the Scc1 substrate that is distinct from the cleavage site and is required for rapid and specific substrate cleavage. Securin also contains a conserved LPE motif, and we provide evidence that this sequence blocks separase engagement of the Scc1 LPE motif. Our results suggest that rapid cohesin cleavage by separase requires a substrate docking interaction outside the active site. This interaction is blocked by securin, providing a second mechanism by which securin inhibits cohesin cleavage.



2019 ◽  
Vol 38 (14) ◽  
pp. 4246-4258 ◽  
Author(s):  
Aina Hazimah Bahaman ◽  
Roswanira Abdul Wahab ◽  
Azzmer Azzar Abdul Hamid ◽  
Khairul Bariyyah Abd Halim ◽  
Yilmaz Kaya ◽  
...  


2019 ◽  
Vol 38 (11) ◽  
pp. 3432-3441 ◽  
Author(s):  
Wafaa Hassan Muslem ◽  
Mohamed Faraj Edbeib ◽  
Hasan Murat Aksoy ◽  
Yilmaz Kaya ◽  
Azzmer Azzar Abdul Hamid ◽  
...  


2019 ◽  
Vol 294 (36) ◽  
pp. 13355-13365 ◽  
Author(s):  
Haiyang Liu ◽  
Zhiwei Li ◽  
Qingqing Yang ◽  
Wei Liu ◽  
Jun Wan ◽  
...  


2019 ◽  
Vol 9 (8) ◽  
pp. 1961-1969 ◽  
Author(s):  
Di-Chen Wang ◽  
Heng Li ◽  
Shu-Ning Xia ◽  
Ya-Ping Xue ◽  
Yu-Guo Zheng

Enzyme–substrate docking-guided point mutation of the substrate-binding pocket to generate mutant L244G/A250G/L245R with superior activity in the synthesis of (R)-2-hydroxy-4-phenylbutyric acid.



2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Nicolina Clemente ◽  
Alaa Abdine ◽  
Iban Ubarretxena-Belandia ◽  
Chunyu Wang


2018 ◽  
Vol 6 (1) ◽  
pp. 1-7
Author(s):  
Rebaone Letsididi ◽  
Kekgabile S. Letsididi ◽  
Tao Zhang ◽  
Bo Jiang ◽  
Wanmeng Mu


Biochimie ◽  
2017 ◽  
Vol 140 ◽  
pp. 166-175 ◽  
Author(s):  
Lionel Ducassou ◽  
Laura Dhers ◽  
Gabriella Jonasson ◽  
Nicolas Pietrancosta ◽  
Jean-Luc Boucher ◽  
...  


2017 ◽  
Vol 420 ◽  
pp. 259-266 ◽  
Author(s):  
Ezhilarasi Krishnamoorthy ◽  
Sameer Hassan ◽  
Luke Elizabeth Hanna ◽  
Indira Padmalayam ◽  
Rama Rajaram ◽  
...  


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