PDBsum entry 4zj9

Chaperone

PDB id: 4zj9

Contents

Protein chain

93 a.a.

Ligands

MPD

Waters ×28

PDB id:

4zj9

Name:

Chaperone

Title:

Small heat shock protein agsa from salmonella typhimurium: alpha crystallin domain

Structure:

Aggregation suppressing protein. Chain: a. Fragment: unp residues 12-147. Engineered: yes

Source:

Salmonella enterica subsp. Enterica serovar typhimurium. Organism_taxid: 90371. Strain: lt2. Gene: agsa. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.00Å R-factor: 0.222 R-free: 0.254

Authors:

N.Mani,K.Suguna

Key ref:

N.Mani et al. (2016). Multiple oligomeric structures of a bacterial small heat shock protein. Sci Rep, 6, 24019. PubMed id: 27053150

Date:

29-Apr-15 Release date: 20-Apr-16

Protein chain

Q8ZPY6  (Q8ZPY6_SALTY) -  Molecular chaperone (Small heat shock protein) from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 155 a.a.

Struc: 93 a.a.

Sci Rep 6:24019 (2016)

PubMed id: 27053150

Multiple oligomeric structures of a bacterial small heat shock protein.

N.Mani, S.Bhandari, R.Moreno, L.Hu, B.V.Prasad, K.Suguna.

ABSTRACT

Small heat shock proteins are ubiquitous molecular chaperones that form the first line of defence against the detrimental effects of cellular stress. Under conditions of stress they undergo drastic conformational rearrangements in order to bind to misfolded substrate proteins and prevent cellular protein aggregation. Owing to the dynamic nature of small heat shock protein oligomers, elucidating the structural basis of chaperone action and oligomerization still remains a challenge. In order to understand the organization of sHSP oligomers, we have determined crystal structures of a small heat shock protein from Salmonella typhimurium in a dimeric form and two higher oligomeric forms: an 18-mer and a 24-mer. Though the core dimer structure is conserved in all the forms, structural heterogeneity arises due to variation in the terminal regions.