Results 101 to 110 of about 3,959 (198)
Superimposition with the NMR structure of the PPIase domain of FKBP38.
, 2017 Superimposition of the PPIase domains from NMR (yellow) and crystallography (green) show that the structures are essentially the same. However, in the crystal structure, relative to that of the NMR structure, a loop is present (Red) that disrupts β ...
Katie L. I. M. Blundell (3826723) +4 more
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BMC Genomics, 2006 Background The peptidyl-prolyl cis/trans isomerase (PPIase) class of proteins is present in all known eukaryotes, prokaryotes, and archaea, and it is comprised of three member families that share the ability to catalyze the cis/trans isomerisation of a ...
Pemberton Trevor J
doaj +1 more source
PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism.
Journal of Biological Chemistry, 1992 FK506-binding protein (FKBP) catalyzes the cis-trans isomerization of the peptidyl-prolyl amide bond (the PPIase reaction) and is the major intracellular receptor for the immunosuppressive drugs FK506 and rapamycin. One mechanism proposed for catalysis of the PPIase reaction requires attack of an enzyme nucleophile on the carbonyl carbon of the ...
S T, Park +4 more
openaire +2 more sources
Dimeric structure of the bacterial extracellular foldase PrsA [PDF]
, 2015 Secretion of proteins into the membrane-cell wall space is essential for cell wall biosynthesis and pathogenicity in Gram-positive bacteria. Folding and maturation of many secreted proteins depend on a single extracellular foldase, the PrsA protein. PrsA
Schmidpeter, Philipp A. M. +7 more
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Non-Catalytic Participation of the Pin1 Peptidyl-Prolyl Isomerase Domain in Target Binding
Frontiers in Physiology, 2013 Pin1 is a phosphorylation-dependent peptidyl-prolyl isomerase that has the potential to add an additional level of regulation within protein kinase mediated signaling pathways.
Brendan Tooke Innes +4 more
doaj +1 more source
, 2020 Consistent with a role in catalyzing rate-limiting step of protein folding, removal of genes encoding cytoplasmic protein folding catalysts belonging to the family of peptidyl-prolyl cis/trans isomerases (PPIs) in Escherichia coli confers conditional ...
Satish Raina +5 more
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BMC Evolutionary Biology, 2006 Background Recently, HEN1 protein from Arabidopsis thaliana was discovered as an essential enzyme in plant microRNA (miRNA) biogenesis. HEN1 transfers a methyl group from S-adenosylmethionine to the 2'-OH or 3'-OH group of the last nucleotide of miRNA ...
Obarska Agnieszka +2 more
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Dual client binding sites in the ATP-independent chaperone SurA
Nature CommunicationsThe ATP-independent chaperone SurA protects unfolded outer membrane proteins (OMPs) from aggregation in the periplasm of Gram-negative bacteria, and delivers them to the β-barrel assembly machinery (BAM) for folding into the outer membrane (OM ...
Bob Schiffrin +11 more
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Struktur und Funktion der Peptidyl-Prolyl-cis/trans-Isomerase-Domäne des humanen FK506-bindenden Proteins 37.7 [PDF]
, 2012 Für das humane FK506-bindende Protein 37.7 wurde eine N-terminal lokalisierte PPIase-Domäne vom FKBP-Typ und eine C-terminal lokalisierte TPR-Domäne vorhergesagt.
Linnert, Miriam
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Activation of Avr3b is dependent on the PPIase activity of GmCYP1.
, 2015 (A) GmCYP1 possesses peptidyl-prolyl cis-trans isomerase (PPlase) activity. GmCYP1R62A (PPIase-deficient mutant) was generated by site-directed mutagenesis. The PPIase enzymatic activity of GST, GmCYP1, and GmCYP1R62A produced in E.
Suomeng Dong (154891) +12 more
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