4N4P

Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form I

Summary for 4N4P

• Entry DOI: 10.2210/pdb4n4p/pdb
• Related: 4N4Q
• Descriptor: Acylneuraminate lyase, CHLORIDE ION (3 entities in total)
• Functional Keywords: tim barrel, lyase
• Biological source: Mycoplasma synoviae
• Total number of polymer chains: 4
• Total formula weight: 134895.25

Authors

Georgescauld, F.,Popova, K.,Gupta, A.J.,Bracher, A.,Engen, J.R.,Hayer-Hartl, M.,Hartl, F.U. (deposition date: 2013-10-08, release date: 2014-05-21, Last modification date: 2023-09-20)

Primary citation

Georgescauld, F.,Popova, K.,Gupta, A.J.,Bracher, A.,Engen, J.R.,Hayer-Hartl, M.,Hartl, F.U.
GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.
Cell(Cambridge,Mass.), 157:922-934, 2014

PubMed Abstract: The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate substrates of GroEL share the (βα)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.

PubMed: 24813614
DOI: 10.1016/j.cell.2014.03.038

Experimental method

X-RAY DIFFRACTION (1.8 Å)