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A mobile loop near the active site acts as a switch between the dual activities of a viral protease/deubiquitinase
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نویسنده
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jupin i. ,ayach m. ,jomat l. ,fieulaine s. ,bressanelli s.
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منبع
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plos pathogens - 2017 - دوره : 13 - شماره : 11
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چکیده
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The positive-strand rna virus turnip yellow mosaic virus (tymv) encodes an ovarian tumor (otu)-like protease/deubiquitinase (pro/dub) protein domain involved both in proteolytic processing of the viral polyprotein through its pro activity,and in removal of ubiquitin chains from ubiquitylated substrates through its dub activity. here,the crystal structures of tymv pro/dub mutants and molecular dynamics simulations reveal that an idiosyncratic mobile loop participates in reversibly constricting its unusual catalytic site by adopting open
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کلیدواژه
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intermediate or closed conformations. The two cis-prolines of the loop form a rigid flap that in the most closed conformation zips up against the other side of the catalytic cleft. The intermediate and closed conformations also correlate with a reordering of the TYMV PRO/DUB catalytic dyad
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آدرس
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institut jacques monod,cnrs—univ paris-diderot,paris, France, institute for integrative biology of the cell,cea—cnrs—univ paris-saclay,gif sur yvette, France, institut jacques monod,cnrs—univ paris-diderot,paris, France, institute for integrative biology of the cell,cea—cnrs—univ paris-saclay,gif sur yvette, France, institute for integrative biology of the cell,cea—cnrs—univ paris-saclay,gif sur yvette, France
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Authors
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