2011
DOI: 10.1016/j.jmb.2011.01.027
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Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26

Abstract: Summary In the cell, protein folding is mediated by folding catalysts and chaperones. The two functions are often linked, especially when the catalytic module forms part of a multidomain protein, as in Methanococcus jannaschii peptidyl-prolyl cis/trans isomerase (PPIase) FKBP26. Here we show that FKBP26 chaperone activity requires both a 50-residue insertion in the catalytic FKBP domain, also called ‘Insert-in-Flap’ or IF domain, and also an 80-residue C-terminal domain. We determined FKBP26 structures from fo… Show more

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Cited by 9 publications
(11 citation statements)
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“…27) and Methanococcus jannaschii ( Mj FKBP26; ref. 28). An alignment of the sequences of all known structures is shown in Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…27) and Methanococcus jannaschii ( Mj FKBP26; ref. 28). An alignment of the sequences of all known structures is shown in Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Indeed, no structure has been determined previously of chaperones of the FKBP‐IF subfamily in complex with a natural substrate. It should, however, be mentioned that some of the crystal contacts in the various Mj FKBP26 crystal forms were suggested to reflect how they bind folding intermediates (28). This protein, however, belongs to the atypical dimeric “long type” of archeal FKBP proteins that appear to be mechanistically distinct from other members of the FKBP‐IF subfamily.…”
Section: Discussionmentioning
confidence: 99%
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“…Despite PPIases being clearly classified as foldases, multidomain PPIases have also been reported to exhibit chaperone functions as indicated by their ability to bind incompletely folded proteins and prevent aggregation [ 17 23 ]. In addition, Wang and Tsou [ 13 ] noted that foldases may also act as chaperones and vice versa.…”
Section: Introductionmentioning
confidence: 99%
“…By definition, PPIases are foldases, which assist in protein folding by catalyzing cis–trans isomerization of X‐Pro peptide bonds. Additionally, PPIases can function as holdases (also called chaperones), which bind to a folding intermediate or misfolded protein and prevent protein aggregation . For example, FKBP22, another cold shock‐induced multidomain PPIase from the psychrophilic bacterium Shewanella sp.…”
Section: Introductionmentioning
confidence: 99%