PDBsum entry 2nwc

Chaperone

PDB id: 2nwc

Contents

Protein chains

(+ 8 more) 524 a.a. *

* Residue conservation analysis

PDB id:

2nwc

Name:

Chaperone

Title:

A 3.02 angstrom crystal structure of wild-type apo groel in a monoclinic space group

Structure:

60 kda chaperonin. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Synonym: protein cpn60, groel protein. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: grol, groel. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.02Å R-factor: 0.228 R-free: 0.263

Authors:

P.D.Kiser,D.T.Lodowski,K.Palczewski

Key ref:

P.D.Kiser et al. (2007). Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 457-461. PubMed id: 17554162 DOI: 10.1107/S1744309107020295

Date:

14-Nov-06 Release date: 22-May-07

Protein chains

P0A6F5  (CH60_ECOLI) -  Chaperonin GroEL from Escherichia coli (strain K12)

Seq: 548 a.a.

Struc: 524 a.a.

Enzyme reactions

• Enzyme class: E.C.5.6.1.7 - chaperonin ATPase.
• Reaction: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide

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

reference

DOI no: 10.1107/S1744309107020295

Acta Crystallogr Sect F Struct Biol Cryst Commun 63:457-461 (2007)

PubMed id: 17554162

Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions.

P.D.Kiser, D.T.Lodowski, K.Palczewski.

ABSTRACT

GroEL is a member of the ATP-dependent chaperonin family that promotes the proper folding of many cytosolic bacterial proteins. The structures of GroEL in a variety of different states have been determined using X-ray crystallography and cryo-electron microscopy. In this study, a 3.02 A crystal structure of the native GroEL complex from Escherichia coli is presented. The complex was purified and crystallized in the absence of potassium ions, which allowed evaluation of the structural changes that may occur in response to cognate potassium-ion binding by comparison to the previously determined wild-type GroEL structure (PDB code 1xck), in which potassium ions were observed in all 14 subunits. In general, the structure is similar to the previously determined wild-type GroEL crystal structure with some differences in regard to temperature-factor distribution.

Selected figure(s)

Figure 1.
Photograph of a GroEL crystal illuminated with polarized light. The crystals in this photograph grew to final size within one week at 277 K in a crystallization solution consisting of 100 mM imidazole pH 8 containing 34%(v/v) MPD and 0.32 M MgCl[2]. The scale bar represents [similar]200 [micro]m. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 June 1; 63(Pt 6): 457–461. Published online 2007 May 5. doi: 10.1107/S1744309107020295. Copyright [copyright] International Union of Crystallography 2007

Figure 2.
Image of a GroEL monomer showing the location of the potassium ion-binding site as well as the regions that were identified as being most flexible in a comparison to the previously determined wild-type GroEL structure (PDB code 1xck). Residues 44 --45, 202 --204 and 260 --268 line the folding cavity, while residues 477 --487 are located on the outside surface near the ATP-binding site and ring --ring interface of the GroEL complex. This figure was generated using PyMOL v.0.99 (DeLano, 2002[triangle]). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 June 1; 63(Pt 6): 457–461. Published online 2007 May 5. doi: 10.1107/S1744309107020295. Copyright [copyright] International Union of Crystallography 2007

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr Sect F Struct Biol Cryst Commun (2007, 63, 457-461) copyright 2007.