This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4n4p
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n4p RCSB], [http://www.ebi.ac.uk/pdbsum/4n4p PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n4p RCSB], [http://www.ebi.ac.uk/pdbsum/4n4p PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate substrates of GroEL share the (betaalpha)8 TIM-barrel fold, but how the chaperonin promotes folding of these proteins is not known. Here, we analyzed the folding of DapA at peptide resolution using hydrogen/deuterium exchange and mass spectrometry. During spontaneous folding, all elements of the DapA TIM barrel acquire structure simultaneously in a process associated with a long search time. In contrast, GroEL/ES accelerates folding more than 30-fold by catalyzing segmental structure formation in the TIM barrel. Segmental structure formation is also observed during the fast spontaneous folding of a structural homolog of DapA from a bacterium that lacks GroEL/ES. Thus, chaperonin independence correlates with folding properties otherwise enforced by protein confinement in the GroEL/ES cage. We suggest that folding catalysis by GroEL/ES is required by a set of proteins to reach native state at a biologically relevant timescale, avoiding aggregation or degradation. | ||
| + | |||
| + | GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding.,Georgescauld F, Popova K, Gupta AJ, Bracher A, Engen JR, Hayer-Hartl M, Hartl FU Cell. 2014 May 8;157(4):922-34. doi: 10.1016/j.cell.2014.03.038. PMID:24813614<ref>PMID:24813614</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:28, 25 June 2014
Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form I
| |||||||||||
