WFRF:(Brandsdal Bjørn O.)
Sökning: WFRF:(Brandsdal Bjørn O.) > Resolving the energ...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03162naa a2200433 4500 | |
| 001 | oai:DiVA.org:uu-77571 | |
| 003 | SwePub | |
| 008 | 060703s2005 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-775712 URI |
| 040 | a (SwePub)uu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Zavialov, Anton V4 aut |
| 245 | 1 0 | a Resolving the energy paradox of chaperone/usher-mediated fibre assembly |
| 264 | 1 | c 2005 |
| 338 | a print2 rdacarrier | |
| 520 | a Periplasmic chaperone/usher machineries are used for assembly of filamentous adhesion organelles of Gram-negative pathogens in a process that has been suggested to be driven by folding energy. Structures of mutant chaperone–subunit complexes revealed a final folding transition (condensation of the subunit hydrophobic core) on the release of organelle subunit from the chaperone–subunit pre-assembly complex and incorporation into the final fibre structure. However, in view of the large interface between chaperone and subunit in the pre-assembly complex and the reported stability of this complex, it is difficult to understand how final folding could release sufficient energy to drive assembly. In the present paper, we show the X-ray structure for a native chaperone–fibre complex that, together with thermodynamic data, shows that the final folding step is indeed an essential component of the assembly process. We show that completion of the hydrophobic core and incorporation into the fibre results in an exceptionally stable module, whereas the chaperone–subunit pre-assembly complex is greatly destabilized by the high-energy conformation of the bound subunit. This difference in stabilities creates a free energy potential that drives fibre formation. | |
| 653 | a Bacterial Proteins/*chemistry/*physiology | |
| 653 | a Models; Molecular | |
| 653 | a Molecular Chaperones/*chemistry/*physiology | |
| 653 | a Organelles/chemistry | |
| 653 | a Protein Conformation | |
| 653 | a Protein Folding | |
| 653 | a Protein Subunits | |
| 653 | a Research Support; Non-U.S. Gov't | |
| 653 | a Thermodynamics | |
| 700 | 1 | a Tischenko, Vladimir M4 aut |
| 700 | 1 | a Fooks, Laura J4 aut |
| 700 | 1 | a Brandsdal, Björn Ou Uppsala universitet,Institutionen för cell- och molekylärbiologi4 aut |
| 700 | 1 | a Åqvist, Johanu Uppsala universitet,Strukturell molekylärbiologi4 aut0 (Swepub:uu)johanaq |
| 700 | 1 | a Zav'yalov, Vladimir P4 aut |
| 700 | 1 | a Macintyre, Sheila4 aut |
| 700 | 1 | a Knight, Stefan Du Department of Molecular Biology, Uppsala Biomedical Center, Swedish University of Agricultural Sciences, Box 590, SE-753 24 Uppsala, Sweden,4 aut0 (Swepub:uu)stkni677 |
| 710 | 2 | a Uppsala universitetb Institutionen för cell- och molekylärbiologi4 org |
| 773 | 0 | t Biochemical Journalg 389:Pt 3, s. 685-694q 389:Pt 3<685-694x 0264-6021x 1470-8728 |
| 856 | 4 | u http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=15799718&dopt=Citation |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-77571 |
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