PDBsum entry 4n4q

Lyase

PDB id: 4n4q

Contents

Protein chains

293 a.a.

Waters ×482

PDB id:

4n4q

Name:

Lyase

Title:

Crystal structure of n-acetylneuraminate lyase from mycoplasma synoviae, crystal form ii

Structure:

Acylneuraminate lyase. Chain: a, b, c, d. Engineered: yes

Source:

Mycoplasma synoviae. Organism_taxid: 262723. Strain: 53. Gene: ms53_0198, nana. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.241 R-free: 0.283

Authors:

F.Georgescauld,K.Popova,A.J.Gupta,A.Bracher,J.R.Engen,M.Hayer-Hartl, F.U.Hartl

Key ref:

F.Georgescauld et al. (2014). GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding. Cell, 157, 922-934. PubMed id: 24813614 DOI: 10.1016/j.cell.2014.03.038

Date:

08-Oct-13 Release date: 21-May-14

Protein chains

Q4A6K4  (Q4A6K4_MYCS5) -  Acylneuraminate lyase from Mycoplasmopsis synoviae (strain 53)

Seq: 296 a.a.

Struc: 293 a.a.

Enzyme reactions

• Enzyme class: E.C.4.1.3.3 - N-acetylneuraminate lyase.
• Reaction: aceneuramate = aldehydo-N-acetyl-D-mannosamine + pyruvate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

DOI no: 10.1016/j.cell.2014.03.038

Cell 157:922-934 (2014)

PubMed id: 24813614

GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.

F.Georgescauld, K.Popova, A.J.Gupta, A.Bracher, J.R.Engen, M.Hayer-Hartl, F.U.Hartl.

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.